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Reviewed, UniProtKB/Swiss-Prot P03366 (POL_HV1B1)

Last modified January 19, 2010. Version 138. Feed History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Gag-Pol polyprotein
Alternative name(s):
    Pr160Gag-Pol
Cleaved into the following 11 chains:
    1- Recommended name:
            Matrix protein p17
                Short name=MA
    2- Recommended name:
            Capsid protein p24
                Short name=CA
    3- Recommended name:
            Spacer peptide p2
    4- Recommended name:
            Nucleocapsid protein p7
                Short name=NC
    5- Recommended name:
            Transframe peptide
                Short name=TF
    6- Recommended name:
            p6-pol
                Short name=p6*
    7- Recommended name:
            Protease
              EC=3.4.23.16
        Alternative name(s):
            Retropepsin
            PR
    8- Recommended name:
            Reverse transcriptase/ribonuclease H
              EC=2.7.7.49
              EC=2.7.7.7
              EC=3.1.26.4
        Alternative name(s):
            p66 RT
    9- Recommended name:
            p51 RT
    10- Recommended name:
            p15
    11- Recommended name:
            Integrase
                Short name=IN
Gene names
Name: gag-pol
OrganismHuman immunodeficiency virus type 1 (isolate BH10 group M subtype B) (HIV-1)
Taxonomic identifier11678 [NCBI]
Taxonomic lineageViruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Primate lentivirus group
Virus hostHomo sapiens (Human) [TaxID: 9606]

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Protein attributes

Sequence length1447 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation By similarity. Ref.11

Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. The second function is to plays a role in nuclear localization of the viral genome at the very start of cell infection. Matrix protein is the part of the pre-integration complex. It binds in the cytoplasm the human BAF protein which prevent autointegration of the viral genome, and might be included in virions at the ration of zero to 3 BAF dimer per virion. The myristoylation signal and the NLS thus exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu By similarity. Ref.11

Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is dissassembled soon after virion entry. Interaction with human PPIA/CYPA protects the virus from restriction by human TRIM5-alpha and from an unknown antiviral activity in human cells. This capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species By similarity. Ref.11

Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity By similarity. Ref.11

The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles By similarity. Ref.11

Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends By similarity. Ref.11

Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allow the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration By similarity. Ref.11

Catalytic activity

Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.

Endonucleolytic cleavage to 5'-phosphomonoester.

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactor

Binds 2 magnesium ions for reverse transcriptase polymerase activity By similarity.

Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding By similarity.

Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions By similarity.

Enzyme regulation

The viral protease is inhibited by many synthetic protease inhibitors (PIs), such as amprenavir, atazanavir, indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. RT can be inhibited either by nucleoside RT inhibitors (NRTIs) or by non nucleoside RT inhibitors (NNRTIs). NRTIs act as chain terminators, whereas NNRTIs inhibit DNA polymerization by binding a small hydrophobic pocket near the RT active site and inducing an allosteric change in this region. Classical NRTIs are abacavir, adefovir (PMEA), didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir (PMPA), zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs are atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266), emivirine (I-EBU), and nevirapine (BI-RG-587). The tritherapies used as a basic effective treatment of AIDS associate two NRTIs and one NNRTI. Use of protease inhibitors in tritherapy regimens permit more ambitious therapeutic strategies By similarity.

Subunit structure

Pre-integration complex interacts with human HMGA1. Matrix protein p17 is a trimer. Interacts with gp120 and human BAF. Capsid is a homodimer. Interacts with human PPIA/CYPA. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. Integrase is a homodimer and possibly can form homotetramer. Integrase interacts with human SMARCB1/INI1 and human PSIP1/LEDGF isoform 1 By similarity.

Subcellular location

Matrix protein p17: Virion Potential. Host nucleus By similarity. Host cytoplasm By similarity. Host cell membrane; Lipid-anchor Potential. Note: Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane By similarity.

Capsid protein p24: Virion Potential.

Nucleocapsid protein p7: Virion Potential.

Reverse transcriptase/ribonuclease H: Virion Potential.

Integrase: Virion Potential. Host nucleus Potential. Host cytoplasm Potential. Note: Nuclear at initial phase, cytoplasmic at assembly Potential.

Domain

The reverse transcriptase/ribonuclease H (RT) is structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accomodating the incoming nucleotide. The RNase H domain stabilizes the association of RT with primer-template By similarity. Ref.19 Ref.29

The tryptophan repeat motif is involved in RT p66/p51 dimerization By similarity. Ref.19 Ref.29

Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein By similarity. Ref.19 Ref.29

Post-translational modification

Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid protein p7 might be further cleaved after virus entry By similarity. Ref.5 Ref.14

Capsid protein p24 is phosphorylated By similarity.

Matrix protein p17 is tyrosine phosphorylated presumably in the virion by a host kinase. This modification targets the matrix protein to the nucleus By similarity.

Miscellaneous

Capsid protein p24 is able to bind macaque TRIM5-alpha or owl monkey TRIMCyp, preventing reverse transcription of the viral genome and succesfull infection of macaque or owl monkey by HIV-1 By similarity.

The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template switching leading to high recombination rate. Recombination mostly occurs between homologous regions of the two copackaged RNA genomes. If these two RNA molecules derive from different viral strains, reverse transcription will give rise to highly recombinated proviral DNAs.

HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K).

Resistance to inhibitors associated with mutations are observed both in viral protease and in reverse transcriptase. Most of the time, single mutations confer only a modest reduction in drug susceptibility. Combination of several mutations is usually required to develop a high-level drug resistance. These mutations are predominantly found in clade B viruses and not in other genotypes. They are listed in the clade B representative isolate HXB2 (AC P04585).

Sequence similarities

Contains 2 CCHC-type zinc fingers.

Contains 1 integrase catalytic domain.

Contains 1 integrase-type DNA-binding domain.

Contains 1 integrase-type zinc finger.

Contains 1 peptidase A2 domain.

Contains 1 reverse transcriptase domain.

Contains 1 RNase H domain.

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Ontologies

Keywords
   Biological processCapsid maturation
DNA integration
DNA recombination
   Cellular componentCapsid protein
Host cell membrane
Host cytoplasm
Host membrane
Host nucleus
Membrane
Virion
   Coding sequence diversityRibosomal frameshifting
   DiseaseAIDS
   DomainRepeat
Zinc-finger
   LigandMagnesium
Metal-binding
RNA-binding
Viral nucleoprotein
Zinc
   Molecular functionAspartyl protease
DNA-directed DNA polymerase
Endonuclease
Hydrolase
Nuclease
Nucleotidyltransferase
Protease
RNA-directed DNA polymerase
Transferase
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Multifunctional enzyme
Gene Ontology (GO)
   Biological processRNA-dependent DNA replication

Inferred from electronic annotation. Source: InterPro

initiation of viral infection

Inferred from Experiment. Source: Reactome

proteolysis

Inferred from electronic annotation. Source: InterPro

provirus integration

Inferred from Experiment. Source: Reactome

viral procapsid maturation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from Experiment. Source: Reactome

host cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

aspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

integrase activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonuclease H activity

Inferred from electronic annotation. Source: EC

structural molecule activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]

Note: Translation results in the formation of the Gag polyprotein most of the time. Ribosomal frameshifting at the gag-pol genes boundary occurs at low frequency and produces the Gag-Pol polyprotein. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Maintenance of a correct Gag to Gag-Pol ratio is essential for RNA dimerization and viral infectivity.
Isoform Gag-Pol polyprotein (identifier: P03366-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced by -1 ribosomal frameshifting.
Isoform Gag polyprotein (identifier: P03347-1)

The sequence of this isoform can be found in the external entry P03347-1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 14471446Gag-Pol polyprotein
PRO_0000261261
Chain2 – 132131Matrix protein p17 By similarity
PRO_0000042285
Chain133 – 363231Capsid protein p24 By similarity
PRO_0000042286
Peptide364 – 37714Spacer peptide p2 By similarity
PRO_0000042287
Chain378 – 43255Nucleocapsid protein p7 By similarity
PRO_0000042288
Peptide433 – 4408Transframe peptide Potential
PRO_0000246710
Chain441 – 50060p6-pol Potential
PRO_0000042289
Chain501 – 59999Protease By similarity
PRO_0000038647
Chain600 – 1159560Reverse transcriptase/ribonuclease H By similarity
PRO_0000042290
Chain600 – 1039440p51 RT By similarity
PRO_0000042291
Chain1040 – 1159120p15
PRO_0000042292
Chain1160 – 1447288Integrase By similarity
PRO_0000042293

Regions

Domain520 – 58970Peptidase A2
Domain643 – 833191Reverse transcriptase
Domain1033 – 1156124RNase H
Domain1213 – 1363151Integrase catalytic
Zinc finger390 – 40718CCHC-type 1
Zinc finger411 – 42818CCHC-type 2
Zinc finger1162 – 120342Integrase-type
DNA binding1382 – 142948Integrase-type
Region826 – 8349RT 'primer grip'
Motif16 – 227Nuclear export signal By similarity
Motif26 – 327Nuclear localization signal By similarity
Motif997 – 101317Tryptophan repeat motif

Sites

Active site5251For protease activity; shared with dimeric partner Ref.7 Ref.16 Ref.58
Metal binding7091Magnesium; catalytic; for reverse transcriptase activity
Metal binding7841Magnesium; catalytic; for reverse transcriptase activity
Metal binding7851Magnesium; catalytic; for reverse transcriptase activity
Metal binding10421Magnesium; catalytic; for RNase H activity Probable
Metal binding10771Magnesium; catalytic; for RNase H activity Probable
Metal binding10971Magnesium; catalytic; for RNase H activity Probable
Metal binding11481Magnesium; catalytic; for RNase H activity Probable
Metal binding12231Magnesium; catalytic; for integrase activity By similarity
Metal binding12751Magnesium; catalytic; for integrase activity By similarity
Site132 – 1332Cleavage; by viral protease By similarity
Site221 – 2222Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA By similarity
Site363 – 3642Cleavage; by viral protease By similarity
Site377 – 3782Cleavage; by viral protease By similarity
Site432 – 4332Cleavage; by viral protease Potential
Site440 – 4412Cleavage; by viral protease
Site500 – 5012Cleavage; by viral protease
Site599 – 6002Cleavage; by viral protease By similarity
Site10001Essential for RT p66/p51 heterodimerization
Site10131Essential for RT p66/p51 heterodimerization
Site1039 – 10402Cleavage; by viral protease; partial
Site1159 – 11602Cleavage; by viral protease By similarity

Amino acid modifications

Modified residue1321Phosphotyrosine; by host By similarity
Lipidation21N-myristoyl glycine; by host By similarity

Natural variations

Natural variant2971V → L in strain: Isolate PV22.
Natural variant4341L → F
Natural variant7711K → R in strain: Isolate PV22.
Natural variant10501K → R in strain: Isolate PV22.
Natural variant10571V → L in strain: Isolate PV22.
Natural variant11111K → Q in strain: Isolate PV22.
Natural variant11281E → Q in strain: Isolate PV22.

Experimental info

Mutagenesis4401F → I: Complete loss of cleavage between NC and TF. Ref.14
Mutagenesis5001F → I: Complete loss of cleavage between TF and p15. Ref.14
Mutagenesis6511P → G: 74% loss of polymerase activity. 86% loss of RNase H activity. Ref.9
Mutagenesis6541P → G: 64% loss of polymerase activity. 57% loss of RNase H activity. Ref.9
Mutagenesis6641K → A: Strong decrease in RT binding affinity for all dNTP substrates and in catalytic efficiency. 100-fold decreased sensitivity to ddNTP inhibitors. Ref.12
Mutagenesis6641K → E: Strong decrease in RT binding affinity for all dNTP substrates and in catalytic efficiency. 100-fold decreased sensitivity to ddNTP inhibitors. Ref.12
Mutagenesis6641K → Q: Strong decrease in RT binding affinity for all dNTP substrates and in catalytic efficiency. 100-fold decreased sensitivity to ddNTP inhibitors. Ref.12
Mutagenesis6641K → R: 10-fold decreased sensitivity to ddATP and ddCTP inhibitors. Ref.12
Mutagenesis6731L → V: No loss of polymerase activity. No loss of RNase H activity. Ref.9
Mutagenesis7091D → A: 5- to 12-fold decrease in affinity for dTTP substrates. Strongly decreased RNA-directed and DNA-directed DNA polymerase activities. No effect on RNase H activity. Loss of pyrophosphorolysis (reverse of the polymerase reaction). Ref.7
Mutagenesis7091D → S: 5- to 12-fold decrease in affinity for dTTP substrates. Strongly decreased RNA-directed DNA polymerase activity. Slightly decreased DNA-directed DNA polymerase activity. No effect on RNase H activity. Loss of pyrophosphorolysis (reverse of the polymerase reaction). Ref.7
Mutagenesis7521W → A: 73% loss of DNA-directed DNA polymerase activity. 70% loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7521W → F: 10% loss of DNA-directed DNA polymerase activity. 22% loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7521W → Y: 58% loss of DNA-directed DNA polymerase activity. 42% loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7551S → A: 74% loss of polymerase activity. 56% loss of RNase H activity. Ref.9
Mutagenesis7551S → G: Complete loss of polymerase activity. No loss of RNase H activity. Ref.9
Mutagenesis7551S → T: Complete loss of polymerase activity. No loss of RNase H activity. Ref.9
Mutagenesis7561P → G: 34% loss of polymerase activity. No loss of RNase H activity. Ref.9
Mutagenesis7661I → A: 71% loss of DNA-directed DNA polymerase activity. 61% loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7661I → D: 16% loss of DNA-directed DNA polymerase activity. 24% loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7661I → L: 80% loss of DNA-directed DNA polymerase activity. 23% loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7661I → T: 34% increase of DNA-directed DNA polymerase activity. 18% increase of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7661I → V: 70% loss of DNA-directed DNA polymerase activity. 64% loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7821Y → A: Almost complete loss of polymerase activity. Ref.10
Mutagenesis7821Y → F: 70% loss of polymerase activity. No loss of polymerase activity; when associated with V-783. Ref.10
Mutagenesis7831M → I: 54% loss of polymerase activity according to PubMed:9533880; increases polymerase activity according to PubMed:9657675. No loss of RNase H activity. Ref.9 Ref.10
Mutagenesis7831M → L: 90% loss of polymerase activity. No loss of RNase H activity. Ref.9 Ref.10
Mutagenesis7831M → V: 58% loss of polymerase activity. No loss of RNase H activity. Ref.9 Ref.10
Mutagenesis7841D → A: Strongly decreased RNA-directed and DNA-directed DNA polymerase activities. No effect on RNase H activity. Ref.7 Ref.10
Mutagenesis7841D → E: Strongly decreased RNA-directed and DNA-directed DNA polymerase activities. No effect on RNase H activity. Ref.7 Ref.10
Mutagenesis7841D → N: Strongly decreased RNA-directed and DNA-directed DNA polymerase activities. No effect on RNase H activity. Ref.7 Ref.10
Mutagenesis7851D → A: Strongly decreased RNA-directed and DNA-directed DNA polymerase activities. Loss of pyrophosphorolysis (reverse of the polymerase reaction). No effect on RNase H activity. Ref.7 Ref.10
Mutagenesis7851D → E: Drastically reduced incorporation of phosphorothioate nucleotide. Loss of pyrophosphorolysis (reverse of the polymerase reaction). No effect on RNase H activity. Ref.7 Ref.10
Mutagenesis7851D → N: Loss of pyrophosphorolysis (reverse of the polymerase reaction). No effect on RNase H activity. Ref.7 Ref.10
Mutagenesis7861L → A: 76% loss of DNA-directed DNA polymerase activity. 60% loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7861L → I: 29% loss of DNA-directed DNA polymerase activity. 46% loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7861L → R: 20% loss of DNA-directed DNA polymerase activity. 21% loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7861L → V: 22% loss of DNA-directed DNA polymerase activity. No loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7881V → A: 37% increase of DNA-directed DNA polymerase activity. No loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7881V → I: 25% increase of DNA-directed DNA polymerase activity. No loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis7881V → M: 27% increase of DNA-directed DNA polymerase activity. 10% loss of RNA-directed DNA polymerase activity. Ref.17
Mutagenesis8231E → A: No effect on RNA-dependent DNA polymerase activity. No effect on RNA 5'-end and 3'-end cleavages. Ref.8
Mutagenesis8241P → A: No effect on RNA-dependent DNA polymerase activity. No effect on RNA 5'-end and 3'-end cleavages. Ref.8
Mutagenesis8251P → A: No effect on RNA-dependent DNA polymerase activity. Complete loss of RNA 5'-end cleavage. No effect on RNA 3'-end cleavage. Ref.8
Mutagenesis8261F → A: No effect on RNA-dependent DNA polymerase activity. Complete loss of RNA 5'-end cleavage. No effect on RNA 3'-end cleavage. Ref.8
Mutagenesis8271L → A: No effect on RNA-dependent DNA polymerase activity. No effect on RNA 5'-end and 3'-end cleavages. Ref.8
Mutagenesis8281W → A: Complete loss of RNA-dependent DNA polymerase activity. No effect on RNA 5'-end and 3'-end cleavages. Ref.8
Mutagenesis8291M → A: No effect on RNA-dependent DNA polymerase activity. No effect on RNA 5'-end and 3'-end cleavages. Ref.8
Mutagenesis8301G → A: Complete loss of RNA-dependent DNA polymerase activity. Complete loss of RNA 5'-end and 3'-end cleavages. Ref.8
Mutagenesis8311Y → A: Complete loss of RNA-dependent DNA polymerase activity. Complete loss of RNA 5'-end and 3'-end cleavages. Ref.8
Mutagenesis8321E → A: Complete loss of RNA-dependent DNA polymerase activity. Complete loss of RNA 5'-end and 3'-end cleavages. Ref.8
Mutagenesis8341H → A: Complete loss of RNA-dependent DNA polymerase activity. Complete loss of RNA 5'-end and 3'-end cleavages. Ref.8
Mutagenesis8561I → T: 96% loss of polymerase activity. 45% loss of RNase H activity. Ref.9
Mutagenesis8611G → A: Complete loss of polymerase activity. 25% loss of RNase H activity. Ref.9
Mutagenesis8631L → S: 17% loss of polymerase activity. 30% loss of RNase H activity. Ref.9
Mutagenesis8651W → T: Complete loss of polymerase activity. 87% loss of RNase H activity. Ref.9
Mutagenesis8781L → S: 21% loss of polymerase activity. 16% loss of RNase H activity. Ref.9
Mutagenesis8981A → L: 68% loss of polymerase activity. 10% loss of RNase H activity. Ref.9
Mutagenesis9021L → S: 59% loss of polymerase activity. 8% loss of RNase H activity. Ref.9
Mutagenesis9091L → S: 31% loss of polymerase activity. No loss of RNase H activity. Ref.9
Mutagenesis9971W → L: No effect on RT p66/p51 heterodimerization. Ref.19
Mutagenesis10001W → A: Almost complete loss of RT p66/p51 heterodimerization. Complete loss of polymerase activity. Ref.19 Ref.21
Mutagenesis10001W → F: No effect on RT p66/p51 heterodimerization. Ref.19 Ref.21
Mutagenesis10001W → L: Almost complete loss of RT p66/p51 heterodimerization. Complete loss of polymerase activity. Ref.19 Ref.21
Mutagenesis10011W → L: No effect on RT p66/p51 heterodimerization. Ref.19
Mutagenesis10041Y → L: No effect on RT p66/p51 heterodimerization. Ref.19
Mutagenesis10051W → L: Decreased RT p66/p51 heterodimerization. Ref.19
Mutagenesis10091W → L: No effect on RT p66/p51 heterodimerization. Ref.19
Mutagenesis10131W → L: Almost complete loss of RT p66/p51 heterodimerization. Ref.19
Mutagenesis10361A → I: Replication slightly delayed. Ref.23
Mutagenesis10371E → N: Virions contain primarily p51 RT. Ref.23
Mutagenesis10381T → S: Almost complete loss of virion production; when associated with G-1041. Ref.23
Mutagenesis10391F → A: Virions contain primarily p51 RT. Ref.5 Ref.23
Mutagenesis10391F → I: Loss of cleavage between p51 RT and p15. Ref.5 Ref.23
Mutagenesis10391F → L: No effect on cleavage between p51 RT and p15. Ref.5 Ref.23
Mutagenesis10391F → V: Slight delays in replication. Virions contain primarily p51 RT. Ref.5 Ref.23
Mutagenesis10391F → W: Slight delays in replication. Virions contain primarily p51 RT. Ref.5 Ref.23
Mutagenesis10401Y → A: Virions contain primarily p51 RT; when associated with A-1039. Ref.23
Mutagenesis10401Y → I: Almost complete loss of virion production; when associated with K-1041. Ref.23
Mutagenesis10401Y → W: Virions contain primarily p51 RT; when associated with W-1039. Ref.23
Mutagenesis10411V → G: Almost complete loss of virion production; when associated with S-1038. Ref.23
Mutagenesis10411V → K: Almost complete loss of virion production; when associated with I-1038. Ref.23
Mutagenesis10411V → S: Slight delays in replication. Ref.23
Mutagenesis10771E → Q: No loss of polymerase activity. complete loss of RNase H activity. Ref.9
Mutagenesis11001Y → A, G, H, L, S or Q: Complete loss of RNAase H activity. Ref.18
Mutagenesis11001Y → E: Almost complete loss of RNAase H activity. Ref.18
Mutagenesis11001Y → F: Almost no effect on RNAase H activity and replication. Ref.18
Mutagenesis11001Y → R: Almost no effect on RNAase H activity. Unable to replicate. Completely resistant to inhibition by BBNH. Ref.18
Mutagenesis11001Y → W: Almost no effect on RNAase H activity and replication. 6-fold resistance to inhibition by BBNH. Ref.18
Mutagenesis11381H → D or N: Severely reduces exonuclease activity of RNase H. Probably also reduces substrate binding affinity. Modifies cleavage preferences of RNase H. No effect on the endonuclease activity. Ref.6
Mutagenesis11381H → D: Severely reduced exonuclease activity of RNase H, but no effect on endonucleonuclease activity. Ref.6
Mutagenesis11381H → N: Severely reduced exonuclease activity of RNase H, but no effect on endonucleonuclease activity. Ref.6
Mutagenesis11591L → F: No effect on cleavage between reverse transcriptase/ribonuclease H and integrase. Ref.5
Mutagenesis11591L → I: Loss of cleavage between reverse transcriptase/ribonuclease H and integrase. Ref.5

Secondary structure

1 ..................................................................................................................... 1447
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform Gag-Pol polyprotein [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AC3EE1439592E0AD

FASTA1,447163,288
        10         20         30         40         50         60 
MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL LETSEGCRQI 

        70         80         90        100        110        120 
LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA LDKIEEEQNK SKKKAQQAAA 

       130        140        150        160        170        180 
DTGHSSQVSQ NYPIVQNIQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT 

       190        200        210        220        230        240 
PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT 

       250        260        270        280        290        300 
STLQEQIGWM TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF 

       310        320        330        340        350        360 
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC QGVGGPGHKA 

       370        380        390        400        410        420 
RVLAEAMSQV TNTATIMMQR GNFRNQRKMV KCFNCGKEGH TARNCRAPRK KGCWKCGKEG 

       430        440        450        460        470        480 
HQMKDCTERQ ANFLREDLAF LQGKAREFSS EQTRANSPTI SSEQTRANSP TRRELQVWGR 

       490        500        510        520        530        540 
DNNSPSEAGA DRQGTVSFNF PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG 

       550        560        570        580        590        600 
RWKPKMIGGI GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNFP 

       610        620        630        640        650        660 
ISPIETVPVK LKPGMDGPKV KQWPLTEEKI KALVEICTEM EKEGKISKIG PENPYNTPVF 

       670        680        690        700        710        720 
AIKKKDSTKW RKLVDFRELN KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD 

       730        740        750        760        770        780 
EDFRKYTAFT IPSINNETPG IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF KKQNPDIVIY 

       790        800        810        820        830        840 
QYMDDLYVGS DLEIGQHRTK IEELRQHLLR WGLTTPDKKH QKEPPFLWMG YELHPDKWTV 

       850        860        870        880        890        900 
QPIVLPEKDS WTVNDIQKLV GKLNWASQIY PGIKVRQLCK LLRGTKALTE VIPLTEEAEL 

       910        920        930        940        950        960 
ELAENREILK EPVHGVYYDP SKDLIAEIQK QGQGQWTYQI YQEPFKNLKT GKYARMRGAH 

       970        980        990       1000       1010       1020 
TNDVKQLTEA VQKITTESIV IWGKTPKFKL PIQKETWETW WTEYWQATWI PEWEFVNTPP 

      1030       1040       1050       1060       1070       1080 
LVKLWYQLEK EPIVGAETFY VDGAANRETK LGKAGYVTNK GRQKVVPLTN TTNQKTELQA 

      1090       1100       1110       1120       1130       1140 
IYLALQDSGL EVNIVTDSQY ALGIIQAQPD KSESELVNQI IEQLIKKEKV YLAWVPAHKG 

      1150       1160       1170       1180       1190       1200 
IGGNEQVDKL VSAGIRKILF LDGIDKAQDE HEKYHSNWRA MASDFNLPPV VAKEIVASCD 

      1210       1220       1230       1240       1250       1260 
KCQLKGEAMH GQVDCSPGIW QLDCTHLEGK VILVAVHVAS GYIEAEVIPA ETGQETAYFL 

      1270       1280       1290       1300       1310       1320 
LKLAGRWPVK TIHTDNGSNF TSATVKAACW WAGIKQEFGI PYNPQSQGVV ESMNKELKKI 

      1330       1340       1350       1360       1370       1380 
IGQVRDQAEH LKTAVQMAVF IHNFKRKGGI GGYSAGERIV DIIATDIQTK ELQKQITKIQ 

      1390       1400       1410       1420       1430       1440 
NFRVYYRDSR NPLWKGPAKL LWKGEGAVVI QDNSDIKVVP RRKAKIIRDY GKQMAGDDCV 


ASRQDED

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Isoform Gag polyprotein.

See P03347.

FASTA––

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References

[1]"Complete nucleotide sequence of the AIDS virus, HTLV-III."
Ratner L., Haseltine W.A., Patarca R., Livak K.J., Starcich B.R., Josephs S.F., Doran E.R., Rafalski J.A., Whitehorn E.A., Baumeister K., Ivanoff L., Petteway S.R. Jr., Pearson M.L., Lautenberger J.A., Papas T.S., Ghrayeb J., Chang N.T., Gallo R.C., Wong-Staal F.
Nature 313:277-284(1985) [PubMed: 2578615] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Nucleic acid structure and expression of the human AIDS/lymphadenopathy retrovirus."
Muesing M.A., Smith D.H., Cabradilla C.D., Benton C.V., Lasky L.A., Capon D.J.
Nature 313:450-458(1985) [PubMed: 2982104] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Isolate PV22.
[3]Muesing M.A.
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"Human immunodeficiency virus reverse transcriptase displays a partially processive 3' to 5' endonuclease activity."
DeStefano J.J., Buiser R.G., Mallaber L.M., Bambara R.A., Fay P.J.
J. Biol. Chem. 266:24295-24301(1991) [PubMed: 1722202] [Abstract]
Cited for: CHARACTERIZATION OF RNASE H.
[5]"Mutating P2 and P1 residues at cleavage junctions in the HIV-1 pol polyprotein. Effects on hydrolysis by HIV-1 proteinase."
Jupp R.A., Phylip L.H., Mills J.S., Le Grice S.F.J., Kay J.
FEBS Lett. 283:180-184(1991) [PubMed: 2044756] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF PHE-1039 AND LEU-1159.
[6]"Mutations of a conserved residue within HIV-1 ribonuclease H affect its exo- and endonuclease activities."
Wohrl B.M., Volkmann S., Moelling K.
J. Mol. Biol. 220:801-818(1991) [PubMed: 1714505] [Abstract]
Cited for: MUTAGENESIS OF HIS-1138.
[7]"Biochemical analysis of catalytically crucial aspartate mutants of human immunodeficiency virus type 1 reverse transcriptase."
Kaushik N., Rege N., Yadav P.N.S., Sarafianos S.G., Modak M.J., Pandey V.N.
Biochemistry 35:11536-11546(1996) [PubMed: 8794733] [Abstract]
Cited for: ACTIVE SITES OF REVERSE TRANSCRIPTASE, MUTAGENESIS OF ASP-709; ASP-784 AND ASP-785.
[8]"Mutations within the primer grip region of HIV-1 reverse transcriptase result in loss of RNase H function."
Palaniappan C., Wisniewski M., Jacques P.S., Le Grice S.F., Fay P.J., Bambara R.A.
J. Biol. Chem. 272:11157-11164(1997) [PubMed: 9111014] [Abstract]
Cited for: MUTAGENESIS OF GLU-823; PRO-824; PRO-825; PHE-826; LEU-827; TRP-828; MET-829; GLY-830; TYR-831; GLU-832 AND HIS-834.
[9]"Effects of mutations in the polymerase domain on the polymerase, RNase H and strand transfer activities of human immunodeficiency virus type 1 reverse transcriptase."
Gao H.-Q., Boyer P.L., Arnold E., Hughes S.H.
J. Mol. Biol. 277:559-572(1998) [PubMed: 9533880] [Abstract]
Cited for: MUTAGENESIS OF PRO-651; PRO-654; LEU-673; SER-755; PRO-756; MET-783; ILE-856; GLY-861; LEU-863; TRP-865; LEU-878; ALA-898; LEU-902; LEU-909 AND GLU-1077.
[10]"Loss of polymerase activity due to Tyr to Phe substitution in the YMDD motif of human immunodeficiency virus type-1 reverse transcriptase is compensated by Met to Val substitution within the same motif."
Harris D., Yadav P.N.S., Pandey V.N.
Biochemistry 37:9630-9640(1998) [PubMed: 9657675] [Abstract]
Cited for: MUTAGENESIS OF TYR-782; MET-783; ASP-784 AND ASP-785.
[11]"Sequence requirements for removal of tRNA by an isolated human immunodeficiency virus type 1 RNase H domain."
Smith C.M., Leon O., Smith J.S., Roth M.J.
J. Virol. 72:6805-6812(1998) [PubMed: 9658129] [Abstract]
Cited for: FUNCTION OF RNASE H.
[12]"Mutational analysis of Lys65 of HIV-1 reverse transcriptase."
Sluis-Cremer N., Arion D., Kaushik N., Lim H., Parniak M.A.
Biochem. J. 348:77-82(2000) [PubMed: 10794716] [Abstract]
Cited for: MUTAGENESIS OF LYS-664.
[13]"Unique progressive cleavage mechanism of HIV reverse transcriptase RNase H."
Wisniewski M., Balakrishnan M., Palaniappan C., Fay P.J., Bambara R.A.
Proc. Natl. Acad. Sci. U.S.A. 97:11978-11983(2000) [PubMed: 11035788] [Abstract]
Cited for: CHARACTERIZATION OF RNASE H.
[14]"Extended nucleocapsid protein is cleaved from the Gag-Pol precursor of human immunodeficiency virus type 1."
Chen N., Morag A., Almog N., Blumenzweig I., Dreazin O., Kotler M.
J. Gen. Virol. 82:581-590(2001) [PubMed: 11172099] [Abstract]
Cited for: RIBOSOMAL FRAMESHIFT, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF PHE-440 AND PHE-500.
[15]"Maintenance of the Gag/Gag-Pol ratio is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity."
Shehu-Xhilaga M., Crowe S.M., Mak J.
J. Virol. 75:1834-1841(2001) [PubMed: 11160682] [Abstract]
Cited for: GAG/GAG-POL RATIO.
[16]"Conformational changes in HIV-1 proteinase: effect of protonation of the active center on conformation of HIV-1 proteinase in water."
Koval'skii D.B., Kanibolotskii D.S., Dubina V.N., Korneliuk A.I.
Ukr. Biokhim. Zh. 74:135-138(2002) [PubMed: 12924029] [Abstract]
Cited for: ACTIVE SITE ASP-525 OF PROTEASE.
[17]"Substitution of conserved hydrophobic residues in motifs B and C of HIV-1 RT alters the geometry of its catalytic pocket."
Sharma B., Kaushik N., Singh K., Kumar S., Pandey V.N.
Biochemistry 41:15685-15697(2002) [PubMed: 12501197] [Abstract]
Cited for: MUTAGENESIS OF TRP-752; ILE-766; LEU-786 AND VAL-788.
[18]"Mutational analysis of Tyr-501 of HIV-1 reverse transcriptase. Effects on ribonuclease H activity and inhibition of this activity by N-acylhydrazones."
Arion D., Sluis-Cremer N., Min K.-L., Abram M.E., Fletcher R.S., Parniak M.A.
J. Biol. Chem. 277:1370-1374(2002) [PubMed: 11684697] [Abstract]
Cited for: MUTAGENESIS OF TYR-1100.
[19]"Role of residues in the tryptophan repeat motif for HIV-1 reverse transcriptase dimerization."
Tachedjian G., Aronson H.-E., de los Santos M., Seehra J., McCoy J.M., Goff S.P.
J. Mol. Biol. 326:381-396(2003) [PubMed: 12559908] [Abstract]
Cited for: DOMAIN TRYPTOPHAN REPEAT MOTIF, MUTAGENESIS OF TRP-997; TRP-1000; TRP-1001; TYR-1004; TRP-1005; TRP-1009 AND TRP-1013.
[20]"Recognition of internal cleavage sites by retroviral RNases H."
Schultz S.J., Zhang M., Champoux J.J.
J. Mol. Biol. 344:635-652(2004) [PubMed: 15533434] [Abstract]
Cited for: CHARACTERIZATION OF RNASE H.
[21]"Relationship between enzyme activity and dimeric structure of recombinant HIV-1 reverse transcriptase."
Tachedjian G., Radzio J., Sluis-Cremer N.
Proteins 60:5-13(2005) [PubMed: 15852304] [Abstract]
Cited for: CHARACTERIZATION OF REVERSE TRANSCRIPTASE, MUTAGENESIS OF TRP-1000.
[22]"Nucleotide modification at the gamma-phosphate leads to the improved fidelity of HIV-1 reverse transcriptase."
Mulder B.A., Anaya S., Yu P., Lee K.W., Nguyen A., Murphy J., Willson R., Briggs J.M., Gao X., Hardin S.H.
Nucleic Acids Res. 33:4865-4873(2005) [PubMed: 16141194] [Abstract]
Cited for: CHARACTERIZATION OF RNASE H.
[23]"Virion instability of human immunodeficiency virus type 1 reverse transcriptase (RT) mutated in the protease cleavage site between RT p51 and the RT RNase H domain."
Abram M.E., Parniak M.A.
J. Virol. 79:11952-11961(2005) [PubMed: 16140771] [Abstract]
Cited for: MUTAGENESIS OF ALA-1036; GLU-1037; THR-1038; PHE-1039; TYR-1040 AND VAL-1041.
[24]"Proteolytic processing and particle maturation."
Vogt V.M.
Curr. Top. Microbiol. Immunol. 214:95-131(1996) [PubMed: 8791726] [Abstract]
Cited for: REVIEW.
[25]"Structural biology of HIV."
Turner B.G., Summers M.F.
J. Mol. Biol. 285:1-32(1999) [PubMed: 9878383] [Abstract]
Cited for: REVIEW.
[26]"Mechanisms of retroviral recombination."
Negroni M., Buc H.
Annu. Rev. Genet. 35:275-302(2001) [PubMed: 11700285] [Abstract]
Cited for: REVIEW.
[27]"Retroviral proteases."
Dunn B.M., Goodenow M.M., Gustchina A., Wlodawer A.
Genome Biol. 3:REVIEWS3006.1-REVIEWS3006.7(2002) [PubMed: 11983066] [Abstract]
Cited for: REVIEW.
[28]"Role of HIV-1 Gag domains in viral assembly."
Scarlata S., Carter C.
Biochim. Biophys. Acta 1614:62-72(2003) [PubMed: 12873766] [Abstract]
Cited for: REVIEW.
[29]"Molecular modeling of the HIV-1 protease and its substrate binding site."
Weber I.T., Miller M., Jaskolski M., Leis J., Skalka A.M., Wlodawer A.
Science 243:928-931(1989) [PubMed: 2537531] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF PROTEASE DOMAIN.
[30]"Recombinant HIV-1 reverse transcriptase: purification, primary structure, and polymerase/ribonuclease H activities."
Mizrahi V., Lazarus G.M., Miles L.M., Meyers C.A., Debouck C.
Arch. Biochem. Biophys. 273:347-358(1989) [PubMed: 2476069] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 600-1159.
[31]"Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor complexed to HIV-1 protease."
Erickson J., Neidhart D.J., Vandrie J., Kempf D.J., Wang X.C., Norbeck D.W., Plattner J.J., Rittenhouse J.W., Turon M., Wideburg N.E., Kohlbrenner W.E., Simmer R., Helfrich R., Paul D.A., Knigge M.
Science 249:527-533(1990) [PubMed: 2200122] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 501-599 IN COMPLEX WITH A C2 SYMMETRIC INHIBITOR.
[32]"Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase."
Davies J.F. II, Hostomska Z., Hostomsky Z., Jordan S.R., Matthews D.A.
Science 252:88-95(1991) [PubMed: 1707186] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1026-1161.
[33]"A recombinant ribonuclease H domain of HIV-1 reverse transcriptase that is enzymatically active."
Evans D.B., Brawn K., Deibel M.R. Jr., Tarpley W.G., Sharma S.K.
J. Biol. Chem. 266:20583-20585(1991) [PubMed: 1718968] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1026-1159.
[34]"Proteolytic release and crystallization of the RNase H domain of human immunodeficiency virus type 1 reverse transcriptase."
Hostomska Z., Matthews D.A., Davies J.F. II, Nodes B.R., Hostomsky Z.
J. Biol. Chem. 266:14697-14702(1991) [PubMed: 1713588] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1026-1161.
[35]"Crystal structure at 3.5-A resolution of HIV-1 reverse transcriptase complexed with an inhibitor."
Kohlstaedt L.A., Wang J., Friedman J.M., Rice P.A., Steitz T.A.
Science 256:1783-1790(1992) [PubMed: 1377403] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 600-1155 IN COMPLEX WITH AN INHIBITOR.
[36]"Structure of HIV-1 reverse transcriptase/DNA complex at 7 A resolution showing active site locations."
Arnold E., Jacobo-Molina A., Nanni R.G., Williams R.L., Lu X., Ding J., Clark A.D. Jr., Zhang A., Ferris A.L., Clark P., Hizi A., Hughes S.H.
Nature 357:85-89(1992) [PubMed: 1374166] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 600-1157.
[37]"A series of penicillin-derived C2-symmetric inhibitors of HIV-1 proteinase: structural and modeling studies."
Wonacott A., Cooke R., Hayes F.R., Hann M.M., Jhoti H., McMeekin P., Mistry A., Murray-Rust P., Singh O.M., Weir M.P.
J. Med. Chem. 36:3113-3119(1993) [PubMed: 8230097] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 501-599.
[38]"A novel constrained reduced-amide inhibitor of HIV-1 protease derived from the sequential incorporation of gamma-turn mimetics into a model substrate."
Newlander K.A., Callahan J.F., Moore M.L., Tomaszek T.A. Jr., Huffman W.F.
J. Med. Chem. 36:2321-2331(1993) [PubMed: 8360876] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 501-599 IN COMPLEX WITH A NOVEL GAMMA-TURN MIMETIC INHIBITOR.
[39]"Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0-A resolution shows bent DNA."
Jacobo-Molina A., Ding J., Nanni R.G., Clark A.D. Jr., Lu X., Tantillo C., Williams R.L., Kamer G., Ferris A.L., Clark P., Hizi A., Hughes S.H., Arnold E.
Proc. Natl. Acad. Sci. U.S.A. 90:6320-6324(1993) [PubMed: 7687065] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 600-1155.
[40]"Structure of the binding site for nonnucleoside inhibitors of the reverse transcriptase of human immunodeficiency virus type 1."
Smerdon S.J., Jager J., Wang J., Kohlstaedt L.A., Chirino A.J., Friedman J.M., Rice P.A., Steitz T.A.
Proc. Natl. Acad. Sci. U.S.A. 91:3911-3915(1994) [PubMed: 7513427] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 600-1159.
[41]"Comparative analysis of the X-ray structures of HIV-1 and HIV-2 proteases in complex with CGP 53820, a novel pseudosymmetric inhibitor."
Priestle J.P., Fassler A., Rosel J., Tintelnot-Blomley M., Strop P., Gruetter M.G.
Structure 3:381-389(1995) [PubMed: 7613867] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 501-599 IN COMPLEX WITH A NOVEL PSEUDOSYMMETRIC INHIBITOR.
[42]"Structure of HIV-1 RT/TIBO R 86183 complex reveals similarity in the binding of diverse nonnucleoside inhibitors."
Ding J., Das K., Moereels H., Koymans L., Andries K., Janssen P.A., Hughes S.H., Arnold E.
Nat. Struct. Biol. 2:407-415(1995) [PubMed: 7545077] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 600-1155 IN COMPLEX WITH A NONNUCLEOSIDE INHIBITOR.
[43]"Structure of HIV-1 reverse transcriptase in a complex with the non-nucleoside inhibitor alpha-APA R 95845 at 2.8-A resolution."
Ding J., Das K., Tantillo C., Zhang W., Clark A.D. Jr., Jessen S., Lu X., Hsiou Y., Jacobo-Molina A., Andries K., Et A.L.
Structure 3:365-379(1995) [PubMed: 7542140] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 600-1157 IN COMPLEX WITH A NON-NUCLEOSIDE INHIBITOR.
[44]"The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1."
Rodgers D.W., Gamblin S.J., Harris B.A., Ray S., Culp J.S., Hellmig B., Woolf D.J., Debouck C., Harrison S.C.
Proc. Natl. Acad. Sci. U.S.A. 92:1222-1226(1995) [PubMed: 7532306] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 600-1159.
[45]"The DNA-binding domain of HIV-1 integrase has an SH3-like fold."
Eijkelenboom A.P.A.M., Lutzke R.A., Boelens R., Plasterk R.H.A., Kaptein R., Hard K.
Nat. Struct. Biol. 2:807-810(1995) [PubMed: 7552753] [Abstract]
Cited for: STRUCTURE BY NMR OF 1379-1429.
[46]"Effect of point mutations on the kinetics and the inhibition of human immunodeficiency virus type 1 protease: relationship to drug resistance."
Lin Y.Z., Lin X.L., Hong L., Foundling S.I., Heinrikson R.L., Thaisrivongs S., Leelamanit W., Raterman D., Shah M., Dunn B.M., Tang J.
Biochemistry 34:1143-1152(1995) [PubMed: 7827064] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE PEPTIDIC INHIBITOR U-89360E.
[47]"Structure of unliganded HIV-1 reverse transcriptase at 2.7-A resolution: implications of conformational changes for polymerization and inhibition mechanisms."
Hsiou Y., Ding J., Das K., Clark A.D. Jr., Hughes S.H., Arnold E.
Structure 4:853-860(1996) [PubMed: 8805568] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 600-1155.
[48]"Unexpected binding mode of a cyclic sulfamide HIV-1 protease inhibitor."
Backbro K., Lowgren S., Osterlund K., Atepo J., Unge T., Hulten J., Bonham N.M., Schaal W., Karlen A., Hallberg A.
J. Med. Chem. 40:898-902(1997) [PubMed: 9083478] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599 IN COMPLEX WITH A SULFAMIDE AND A UREA DERIVATIVE.
[49]"Molecular basis of HIV-1 protease drug resistance: structural analysis of mutant proteases complexed with cyclic urea inhibitors."
Ala P.J., Huston E.E., Klabe R.M., McCabe D.D., Duke J.L., Rizzo C.J., Korant B.D., DeLoskey R.J., Lam P.Y.S., Hodge C.N., Chang C.-H.
Biochemistry 36:1573-1580(1997) [PubMed: 9048541] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 502-599 IN COMPLEX WITH A CYCLIC UREA INHIBITOR.
[50]"Structure of a G48H mutant of HIV-1 protease explains how glycine-48 replacements produce mutants resistant to inhibitor drugs."
Hong L., Zhang X.-J., Foundling S.I., Hartsuck J.A., Tang J.
FEBS Lett. 420:11-16(1997) [PubMed: 9450540] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE PEPTIDIC INHIBITOR U-89360E.
[51]"An orally bioavailable pyrrolinone inhibitor of HIV-1 protease: computational analysis and X-ray crystal structure of the enzyme complex."
Smith A.B. III, Hirschmann R., Pasternak A., Yao W., Sprengeler P.A., Holloway M.K., Kuo L.C., Chen Z., Darke P.L., Schleif W.A.
J. Med. Chem. 40:2440-2444(1997) [PubMed: 9258349] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599.
[52]"Active-site mobility in human immunodeficiency virus, type 1, protease as demonstrated by crystal structure of A28S mutant."
Hong L., Hartsuck J.A., Foundling S.I., Ermolieff J., Tang J.
Protein Sci. 7:300-305(1998) [PubMed: 9521105] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599 IN COMPLEX WITH A PEPTIDIC INHIBITOR.
[53]"Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance."
Huang H., Chopra R., Verdine G.L., Harrison S.C.
Science 282:1669-1675(1998) [PubMed: 9831551] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 588-1027.
[54]"The structure of HIV-1 reverse transcriptase complexed with an RNA pseudoknot inhibitor."
Jaeger J., Restle T., Steitz T.A.
EMBO J. 17:4535-4542(1998) [PubMed: 9687519] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.75 ANGSTROMS) OF 600-1153 IN COMPLEX WITH AN RNA PSEUDOKNOT INHIBITOR.
[55]"Structures of Tyr188Leu mutant and wild-type HIV-1 reverse transcriptase complexed with the non-nucleoside inhibitor HBY 097: inhibitor flexibility is a useful design feature for reducing drug resistance."
Hsiou Y., Das K., Ding J., Clark A.D. Jr., Kleim J.P., Rosner M., Winkler I., Riess G., Hughes S.H., Arnold E.
J. Mol. Biol. 284:313-323(1998) [PubMed: 9813120] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 600-1155 IN COMPLEX WITH A NON-NUCLEOSIDE INHIBITOR.
[56]"Lamivudine (3TC) resistance in HIV-1 reverse transcriptase involves steric hindrance with beta-branched amino acids."
Sarafianos S.G., Das K., Clark A.D. Jr., Ding J., Boyer P.L., Hughes S.H., Arnold E.
Proc. Natl. Acad. Sci. U.S.A. 96:10027-10032(1999) [PubMed: 10468556] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 600-1157.
[57]"Urea-PETT compounds as a new class of HIV-1 reverse transcriptase inhibitors. 3. Synthesis and further structure-activity relationship studies of PETT analogues."
Hogberg M., Sahlberg C., Engelhardt P., Noreen R., Kangasmetsa J., Johansson N.G., Oberg B., Vrang L., Zhang H., Sahlberg B.L., Unge T., Lovgren S., Fridborg K., Backbro K.
J. Med. Chem. 43:304-304(2000) [PubMed: 10650066] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 600-1156.
[58]"Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA."
Sarafianos S.G., Das K., Tantillo C., Clark A.D. Jr., Ding J., Whitcomb J.M., Boyer P.L., Hughes S.H., Arnold E.
EMBO J. 20:1449-1461(2001) [PubMed: 11250910] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 600-1152 IN COMPLEX WITH AN OLIGONUCLEOTIDE, ACTIVE SITES OF RNASE H.
[59]"The Lys103Asn mutation of HIV-1 RT: a novel mechanism of drug resistance."
Hsiou Y., Ding J., Das K., Clark A.D. Jr., Boyer P.L., Lewi P., Janssen P.A., Kleim J.P., Rosner M., Hughes S.H., Arnold E.
J. Mol. Biol. 309:437-445(2001) [PubMed: 11371163] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 600-1159.
[60]"Structures of HIV-1 reverse transcriptase with pre- and post-translocation AZTMP-terminated DNA."
Sarafianos S.G., Clark A.D. Jr., Das K., Tuske S., Birktoft J.J., Ilankumaran P., Ramesha A.R., Sayer J.M., Jerina D.M., Boyer P.L., Hughes S.H., Arnold E.
EMBO J. 21:6614-6624(2002) [PubMed: 12456667] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 600-1157.
[61]"Structural basis for the inhibitory efficacy of efavirenz (DMP-266), MSC194 and PNU142721 towards the HIV-1 RT K103N mutant."
Lindberg J., Sigurdsson S., Lowgren S., Andersson H.O., Sahlberg C., Noreen R., Fridborg K., Zhang H., Unge T.
Eur. J. Biochem. 269:1670-1677(2002) [PubMed: 11895437] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 600-1159 IN COMPLEX WITH EFIVARENZ.
[62]"Optimization of P1-P3 groups in symmetric and asymmetric HIV-1 protease inhibitors."
Andersson H.O., Fridborg K., Lowgren S., Alterman M., Muhlman A., Bjorsne M., Garg N., Kvarnstrom I., Schaal W., Classon B., Karlen A., Danielsson U.H., Ahlsen G., Nillroth U., Vrang L., Oberg B., Samuelsson B., Hallberg A., Unge T.
Eur. J. Biochem. 270:1746-1758(2003) [PubMed: 12694187] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 501-599.
[63]"Design, synthesis, and biological evaluation of monopyrrolinone-based HIV-1 protease inhibitors."
Smith A.B. III, Cantin L.D., Pasternak A., Guise-Zawacki L., Yao W., Charnley A.K., Barbosa J., Sprengeler P.A., Hirschmann R., Munshi S., Olsen D.B., Schleif W.A., Kuo L.C.
J. Med. Chem. 46:1831-1844(2003) [PubMed: 12723947] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599 IN COMPLEX WITH MONOPYRROLINONE-BASED INHIBITORS LDC271 AND LGZ479.
[64]"Symmetric fluoro-substituted diol-based HIV protease inhibitors. Ortho-fluorinated and meta-fluorinated P1/P1'-benzyloxy side groups significantly improve the antiviral activity and preserve binding efficacy."
Lindberg J., Pyring D., Lowgren S., Rosenquist A., Zuccarello G., Kvarnstrom I., Zhang H., Vrang L., Classon B., Hallberg A., Samuelsson B., Unge T.
Eur. J. Biochem. 271:4594-4602(2004) [PubMed: 15560801] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 501-599.
[65]"Nonnucleoside inhibitor binding affects the interactions of the fingers subdomain of human immunodeficiency virus type 1 reverse transcriptase with DNA."
Peletskaya E.N., Kogon A.A., Tuske S., Arnold E., Hughes S.H.
J. Virol. 78:3387-3397(2004) [PubMed: 15016861] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 600-1157.
[66]"Structures of HIV-1 RT-DNA complexes before and after incorporation of the anti-AIDS drug tenofovir."
Tuske S., Sarafianos S.G., Clark A.D. Jr., Ding J., Naeger L.K., White K.L., Miller M.D., Gibbs C.S., Boyer P.L., Clark P., Wang G., Gaffney B.L., Jones R.A., Jerina D.M., Hughes S.H., Arnold E.
Nat. Struct. Mol. Biol. 11:469-474(2004) [PubMed: 15107837] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 600-1157 IN COMPLEX WITH DNA BOUND TO TENOFOVIR.
[67]"Synthesis and antiviral activity of P1' arylsulfonamide azacyclic urea HIV protease inhibitors."
Huang P.P., Randolph J.T., Klein L.L., Vasavanonda S., Dekhtyar T., Stoll V.S., Kempf D.J.
Bioorg. Med. Chem. Lett. 14:4075-4078(2004) [PubMed: 15225729] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 501-599 IN COMPLEX WITH ARYLSULFONAMIDE AZACYCLIC UREA INHIBITORS.
[68]"Oximinoarylsulfonamides as potent HIV protease inhibitors."
Yeung C.M., Klein L.L., Flentge C.A., Randolph J.T., Zhao C., Sun M., Dekhtyar T., Stoll V.S., Kempf D.J.
Bioorg. Med. Chem. Lett. 15:2275-2278(2005) [PubMed: 15837308] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 501-599 IN COMPLEX WITH OXIMINOARYLSULFONAMIDE INHIBITOR.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M15654 Genomic RNA. Translation: AAA44198.1. Sequence problems.
K02083 Genomic DNA. Translation: AAB59867.1. Sequence problems.
X01762 Genomic RNA. No translation available.
PIRGNVWH3. A03965.
GNVWVL. A03967.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A9MX-ray2.30A/B501-599[»]
1AJVX-ray2.00A/B501-599[»]
1AJXX-ray2.00A/B501-599[»]
1AXAX-ray2.00A/B501-599[»]
1BQMX-ray3.10A600-1155[»]
B600-1029[»]
1BQNX-ray3.30A600-1157[»]
B600-1029[»]
1D4HX-ray1.81A/B501-599[»]
1D4IX-ray1.81A/B501-599[»]
1D4JX-ray1.81A/B501-599[»]
1DLOX-ray2.70A600-1155[»]
B600-1026[»]
1DW6X-ray1.88C/D501-599[»]
1EBKX-ray2.06C/D/E/F501-599[»]
1EBWX-ray1.81A/B501-599[»]
1EBYX-ray2.29A/B501-599[»]
1EBZX-ray2.01A/B501-599[»]
1EC0X-ray1.79A/B501-599[»]
1EC1X-ray2.10A/B501-599[»]
1EC2X-ray2.00A/B501-599[»]
1EC3X-ray1.80A/B501-599[»]
1EETX-ray2.73A600-1155[»]
B600-1025[»]
1G35X-ray1.80A/B501-599[»]
1GNMX-ray2.30A/B501-599[»]
1GNNX-ray2.30A/B501-599[»]
1GNOX-ray2.30A/B501-599[»]
1HARX-ray2.20A600-815[»]
1HBVX-ray2.30A/B501-599[»]
1HEFX-ray2.20E501-599[»]
1HEGX-ray2.20E501-599[»]
1HIHX-ray2.20A/B501-599[»]
1HMVX-ray3.20A/C/E/G600-1159[»]
B/D/F/H600-1039[»]
1HNIX-ray2.80A600-1157[»]
1HNVX-ray3.00A600-1157[»]
B600-1026[»]
1HOSX-ray2.30A/B501-599[»]
1HPSX-ray2.30A/B501-599[»]
1HPZX-ray3.00A600-1159[»]
B600-1029[»]
1HQEX-ray2.70A600-1159[»]
B600-1029[»]
1HQUX-ray2.70A600-1159[»]
B600-1029[»]
1HRHX-ray2.40A/B1026-1161[»]
1HTEX-ray2.80A/B501-599[»]
1HTFX-ray2.20A/B501-599[»]
1HTGX-ray2.00A/B501-599[»]
1HVIX-ray1.80A/B501-599[»]
1HVKX-ray1.80A/B501-599[»]
1HVPmodel-A/B501-599[»]
1HVUX-ray4.75A/D/G/J600-1153[»]
B/E/H/K604-1026[»]
1HYSX-ray3.00A600-1152[»]
B600-1024[»]
1IKVX-ray3.00A600-1159[»]
B600-1026[»]
1IKWX-ray3.00A600-1159[»]
B600-1026[»]
1IKXX-ray2.80A600-1159[»]
B600-1026[»]
1IKYX-ray3.00A600-1159[»]
B600-1026[»]
1J5OX-ray3.50A600-1157[»]
B600-1029[»]
1KJHX-ray2.00P1154-1163[»]
1MERX-ray1.90A/B501-599[»]
1MESX-ray1.90A/B501-599[»]
1METX-ray1.90A/B501-599[»]
1MEUX-ray1.90A/B501-599[»]
1N5YX-ray3.10A600-1157[»]
B600-1029[»]
1N6QX-ray3.00A600-1157[»]
B600-1029[»]
1NPAX-ray2.00A/B501-599[»]
1NPVX-ray2.00A/B501-599[»]
1NPWX-ray2.00A/B501-599[»]
1QE1X-ray2.85A600-1157[»]
B600-1026[»]
1QMCNMR-A/B1379-1429[»]
1R0AX-ray2.80A600-1157[»]
B600-1028[»]
1RDHX-ray2.80A/B1026-1159[»]
1RTDX-ray3.20A/C601-1153[»]
1RVLmodel-A600-1155[»]
B600-1027[»]
1RVMmodel-A600-1155[»]
B600-1027[»]
1RVNmodel-A600-1155[»]
B600-1027[»]
1RVOmodel-A600-1155[»]
B600-1027[»]
1RVPmodel-A600-1155[»]
B600-1027[»]
1RVQmodel-A600-1155[»]
B600-1027[»]
1RVRmodel-A600-1155[»]
B600-1027[»]
1S6PX-ray2.90A600-1159[»]
B600-1029[»]
1S6QX-ray3.00A600-1159[»]
B600-1029[»]
1S9EX-ray2.60A600-1159[»]
B600-1029[»]
1S9GX-ray2.80A600-1159[»]
B600-1029[»]
1SBGX-ray2.30A/B501-599[»]
1SUQX-ray3.00A600-1159[»]
B600-1029[»]
1SV5X-ray2.90A600-1159[»]
B600-1029[»]
1T03X-ray3.10A600-1157[»]
B600-1028[»]
1T05X-ray3.00A600-1157[»]
1T7KX-ray2.10A/B501-599[»]
1TV6X-ray2.80A600-1159[»]
B600-1039[»]
1TVRX-ray3.00A600-1156[»]
B600-1025[»]
1UWBX-ray3.20A600-1156[»]
B600-1025[»]
1W5VX-ray1.80A/B490-599[»]
1W5WX-ray1.80A/B490-599[»]
1W5XX-ray1.90A/B490-599[»]
1W5YX-ray1.90A/B490-599[»]
1YT9X-ray3.00A/B501-599[»]
1ZP8X-ray2.02A501-599[»]
1ZPAX-ray2.02A501-599[»]
1ZSFX-ray1.98A-[»]
1ZSRX-ray2.06A-[»]
2AQUX-ray2.00A/B501-599[»]
2B5JX-ray2.90A600-1158[»]
B600-1028[»]
2B6AX-ray2.65A600-1158[»]
B600-1028[»]
2BANX-ray2.95A600-1158[»]
B600-1028[»]
2BB9X-ray1.35A/B-[»]
2BBBX-ray1.70A/B-[»]
2BE2X-ray2.43A600-1158[»]
B600-1028[»]
2EXFNMR-A389-431[»]
2G69X-ray1.35A501-599[»]
2HB3X-ray1.35A/B501-598[»]
2HMIX-ray2.80A600-1156[»]
B600-1028[»]
2HNZX-ray3.00B606-1027[»]
2HS1X-ray0.84A/B501-599[»]
2HS2X-ray1.22A/B501-599[»]
2I4DX-ray1.50A/B501-599[»]
2I4UX-ray1.50A/B501-599[»]
2I4VX-ray1.50A/B501-599[»]
2I4WX-ray1.55A/B501-599[»]
2I4XX-ray1.55A/B501-599[»]
2I5JX-ray3.15A600-1150[»]
B600-1027[»]
2IAJX-ray2.50A600-1158[»]
B600-1045[»]
2IC3X-ray3.00A600-1158[»]
B600-1045[»]
2IDWX-ray1.10A/B501-599[»]
2IEOX-ray1.53A/B501-599[»]
2UXZX-ray1.75A/B501-599[»]
2UY0X-ray1.76A/B501-599[»]
2VG5X-ray2.80A600-1156[»]
B600-1027[»]
2VG6X-ray3.01A600-1156[»]
B600-1027[»]
2VG7X-ray2.82A600-1156[»]
B600-1027[»]
2ZD1X-ray1.80A600-1154[»]
B600-1027[»]
2ZE2X-ray2.90A600-1154[»]
B600-1027[»]
3BGRX-ray2.10A600-1154[»]
B600-1027[»]
3DLKX-ray1.85A600-1154[»]
B605-1027[»]
3GGAX-ray2.50A/B/C/D/G/H501-599[»]
3GGVX-ray3.09A/B/C/D/E/F/G/H/I501-599[»]
3GGXX-ray2.70A/B/C/D/E/F/G/H501-599[»]
3HVTX-ray2.90A600-1155[»]
B600-1027[»]
3JSMX-ray3.00A600-1157[»]
B600-1028[»]
3JYTX-ray3.30A600-1157[»]
B600-1028[»]
3TLHX-ray2.00A501-599[»]
ModBaseSearch...

Enzyme and pathway databases

ReactomeREACT_6185. HIV Infection.

Family and domain databases

InterProIPR000721. Gag_p24.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR017856. Integrase_Zn-bd_dom-like_N.
IPR003308. Integrase_Zn-bd_dom_N.
IPR000071. Lentvrl_matrix_N.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
IPR012337. PolynucTfrase_RNaseH_fold.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR000477. Reverse_transcriptase.
IPR002156. RNase_H.
IPR010659. RVT_connect.
IPR010661. RVT_thumb.
IPR013084. Znf_CCH_retrovir.
IPR001878. Znf_CCHC.
[Graphical view]
Gene3DG3DSA:2.30.30.10. Integrase_C. 1 hit.
G3DSA:1.10.10.200. Intgrase_N_Zn_bd. 1 hit.
G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
G3DSA:1.10.1200.30. Retrov_capsid_C. 1 hit.
G3DSA:1.10.375.10. Retrov_capsid_N. 1 hit.
G3DSA:4.10.60.10. Znf_CCH_retrovir. 1 hit.
PfamPF00540. Gag_p17. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00552. Integrase. 1 hit.
PF02022. Integrase_Zn. 1 hit.
PF00075. RnaseH. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF06815. RVT_connect. 1 hit.
PF06817. RVT_thumb. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view]
PRINTSPR00234. HIV1MATRIX.
SMARTSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
PROSITEPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS51027. INTEGRASE_DBD. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
PS50158. ZF_CCHC. 2 hits.
PS50876. ZF_INTEGRASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01264. Darunavir.
DB01093. Dimethyl sulfoxide.
DB01601. Lopinavir.

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Entry information

Entry namePOL_HV1B1
AccessionPrimary (citable) accession number: P03366
Secondary accession number(s): P03368
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectVirus (Virus annotation project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents