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P35961

- ENV_HV1Y2

UniProt

P35961 - ENV_HV1Y2

Protein

Envelope glycoprotein gp160

Gene

env

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate YU-2) (HIV-1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. Since CD4 also displays a binding site for the disulfide-isomerase P4HB/PDI, a P4HB/PDI-CD4-CXCR4-gp120 complex may form. In that complex, P4HB/PDI could reach and reduce gp120 disulfide bonds, causing major conformational changes in gp120. TXN, another PDI family member could also be involved in disulfide rearrangements in Env during fusion. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide.
    Surface protein gp120 (SU) may target the virus to gut-associated lymphoid tissue (GALT) by binding host ITGA4/ITGB7 (alpha-4/beta-7 integrins), a complex that mediates T-cell migration to the GALT. Interaction between gp120 and ITGA4/ITGB7 would allow the virus to enter GALT early in the infection, infecting and killing most of GALT's resting CD4+ T-cells. This T-cell depletion is believed to be the major insult to the host immune system leading to AIDS By similarity.By similarity
    The surface protein gp120 is a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they take up antigen, process it, and present it to T-cells following migration to lymphoid organs. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. Virion capture also seems to lead to MHC-II-restricted viral antigen presentation, and probably to the activation of HIV-specific CD4+ cells By similarity.By similarity
    The transmembrane protein gp41 (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm By similarity.By similarity
    The envelope glyprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface.By similarity
    The gp120-gp41 heterodimer seems to contribute to T-cell depletion during HIV-1 infection. The envelope glycoproteins expressed on the surface of infected cells induce apoptosis through an interaction with uninfected cells expressing the receptor (CD4) and the coreceptors CXCR4 or CCR5. This type of bystander killing may be obtained by at least three distinct mechanisms. First, the interaction between the 2 cells can induce cellular fusion followed by nuclear fusion within the syncytium. Syncytia are condemned to die from apoptosis. Second, the 2 interacting cells may not fuse entirely and simply exchange plasma membrane lipids, after a sort of hemifusion process, followed by rapid death. Third, it is possible that virus-infected cells, on the point of undergoing apoptosis, fuse with CD4-expressing cells, in which case apoptosis is rapidly transmitted from one cell to the other and thus occurs in a sort of contagious fashion By similarity.By similarity
    The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei498 – 4992Cleavage; by host furinBy similarity

    GO - Molecular functioni

    1. structural molecule activity Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
    3. evasion or tolerance by virus of host immune response Source: UniProtKB-KW
    4. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
    5. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Biological processi

    Apoptosis, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Envelope glycoprotein gp160
    Alternative name(s):
    Env polyprotein
    Cleaved into the following 2 chains:
    Surface protein gp120
    Short name:
    SU
    Alternative name(s):
    Glycoprotein 120
    Short name:
    gp120
    Alternative name(s):
    Glycoprotein 41
    Short name:
    gp41
    Gene namesi
    Name:env
    OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate YU-2) (HIV-1)
    Taxonomic identifieri362651 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007419: Genome

    Subcellular locationi

    Chain Transmembrane protein gp41 : Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein. Host endosome membrane Curated; Single-pass type I membrane protein Curated
    Note: It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag.
    Chain Surface protein gp120 : Virion membrane; Peripheral membrane protein. Host cell membrane; Peripheral membrane protein. Host endosome membrane Curated; Peripheral membrane protein Curated
    Note: The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag.

    GO - Cellular componenti

    1. host cell endosome membrane Source: UniProtKB-SubCell
    2. host cell plasma membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. viral envelope Source: UniProtKB-KW
    5. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cell membrane, Host endosome, Host membrane, Membrane, Viral envelope protein, Virion

    Pathology & Biotechi

    Keywords - Diseasei

    AIDS

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131By similarityAdd
    BLAST
    Chaini32 – 843812Envelope glycoprotein gp160PRO_0000239469Add
    BLAST
    Chaini32 – 498467Surface protein gp120By similarityPRO_0000038377Add
    BLAST
    Chaini499 – 843345Transmembrane protein gp41By similarityPRO_0000038378Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi53 ↔ 73By similarity
    Glycosylationi87 – 871N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi118 ↔ 201By similarity
    Disulfide bondi125 ↔ 192By similarity
    Glycosylationi129 – 1291N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi130 ↔ 155By similarity
    Glycosylationi135 – 1351N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi138 – 1381N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi154 – 1541N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi158 – 1581N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi184 – 1841N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi193 – 1931N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi214 ↔ 243By similarity
    Disulfide bondi224 ↔ 235By similarity
    Glycosylationi230 – 2301N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi237 – 2371N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi258 – 2581N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi272 – 2721N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi285 – 2851N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi291 – 2911N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi292 ↔ 326By similarity
    Glycosylationi297 – 2971N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi327 – 3271N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi351 – 3511N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi373 ↔ 432By similarity
    Disulfide bondi380 ↔ 405By similarity
    Glycosylationi381 – 3811N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi389 – 3891N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi400 – 4001N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi435 – 4351N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi450 – 4501N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi598 – 5981N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi603 – 6031N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi612 – 6121N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi624 – 6241N-linked (GlcNAc...); by hostSequence Analysis
    Lipidationi751 – 7511S-palmitoyl cysteine; by hostBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as a inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CD4 receptor By similarity.By similarity
    Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Interactioni

    Subunit structurei

    The mature envelope protein (Env) consists of a homotrimer of non-covalently associated gp120-gp41 heterodimers. The resulting complex protrudes from the virus surface as a spike. There seems to be as few as 10 spikes on the average virion. Surface protein gp120 interacts with human CD4, CCR5 and CXCR4, to form a P4HB/PDI-CD4-CXCR4-gp120 complex. Gp120 also interacts with the C-type lectins CD209/DC-SIGN and CLEC4M/DC-SIGNR (collectively referred to as DC-SIGN(R)). Gp120 and gp41 interact with GalCer. Gp120 interacts with human ITGA4/ITGB7 complex; on CD4+ T-cells, this interaction results in rapid activation of integrin ITGAL/LFA-1, which facilitate efficient cell-to-cell spreading of HIV-1. Gp120 interacts with cell-associated heparan sulfate; this interaction increases virus infectivity on permissive cells and may be involved in infection of CD4- cells By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-48439N.

    Structurei

    Secondary structure

    1
    843
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi52 – 554
    Beta strandi59 – 613
    Helixi64 – 729
    Beta strandi73 – 753
    Beta strandi82 – 843
    Beta strandi90 – 934
    Helixi94 – 963
    Helixi98 – 11417
    Beta strandi118 – 1225
    Beta strandi127 – 1293
    Beta strandi195 – 1984
    Beta strandi201 – 2044
    Beta strandi211 – 2144
    Beta strandi219 – 2246
    Beta strandi231 – 24313
    Beta strandi252 – 2587
    Beta strandi263 – 2653
    Beta strandi267 – 2693
    Beta strandi276 – 2783
    Beta strandi280 – 29415
    Beta strandi298 – 3003
    Turni306 – 3083
    Beta strandi323 – 3297
    Helixi330 – 34819
    Beta strandi350 – 3523
    Beta strandi353 – 3564
    Beta strandi359 – 3613
    Helixi364 – 3674
    Beta strandi369 – 3735
    Beta strandi376 – 3805
    Helixi383 – 3853
    Beta strandi388 – 3914
    Turni396 – 3983
    Beta strandi400 – 41213
    Beta strandi414 – 4218
    Beta strandi426 – 4294
    Beta strandi430 – 44314
    Beta strandi446 – 4494
    Beta strandi452 – 4576
    Helixi462 – 4709
    Beta strandi473 – 4775

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G9NX-ray2.90G82-479[»]
    1RZKX-ray2.90G82-479[»]
    1YYLX-ray2.75G/P82-479[»]
    1YYMX-ray2.20G/P82-479[»]
    2I5YX-ray2.20G/P82-479[»]
    2I60X-ray2.40G/P82-479[»]
    2NY7X-ray2.30G158-479[»]
    2QADX-ray3.30A/E88-479[»]
    3HI1X-ray2.90G/J89-479[»]
    3TGQX-ray3.40A/B/C/D43-479[»]
    4DVRX-ray2.50G82-479[»]
    4JO3X-ray2.60P/Q313-327[»]
    4JZWX-ray1.78A/G43-479[»]
    4JZZX-ray1.49A43-479[»]
    4K0AX-ray2.13A43-479[»]
    4KA2X-ray1.79A43-479[»]
    4LAJX-ray2.14A/B/F/J43-479[»]
    ProteinModelPortaliP35961.
    SMRiP35961. Positions 89-122, 195-479, 499-652.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35961.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 671640ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini693 – 843151CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei672 – 69221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni130 – 15425V1Add
    BLAST
    Regioni155 – 19238V2Add
    BLAST
    Regioni292 – 32534V3Add
    BLAST
    Regioni359 – 36911CD4-binding loopBy similarityAdd
    BLAST
    Regioni380 – 40526V4Add
    BLAST
    Regioni448 – 45811V5Add
    BLAST
    Regioni499 – 51921Fusion peptideSequence AnalysisAdd
    BLAST
    Regioni525 – 54117ImmunosuppressionBy similarityAdd
    BLAST
    Regioni649 – 67022MPER; binding to GalCerBy similarityAdd
    BLAST
    Regioni649 – 6546Involved in GalCer bindingBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili632 – 65221Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi699 – 7024YXXL motif; contains endocytosis signalBy similarity
    Motifi842 – 8432Di-leucine internalization motifBy similarity

    Domaini

    The YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis. YXXL and di-leucine endocytosis motifs interact directly or indirectly with the clathrin adapter complexes, opperate independently, and their activities are not additive By similarity.By similarity
    The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo By similarity.By similarity
    Some of the most genetically diverse regions of the viral genome are present in Env. They are called variable regions 1 through 5 (V1 through V5). Coreceptor usage of gp120 is determined mainly by the primary structure of the third variable region (V3) in the outer domain of gp120. The sequence of V3 determines which coreceptor, CCR5 and/or CXCR4 (corresponding to R5/macrophage, X4/T cell and R5X4/T cell and macrophage tropism), is used to trigger the fusion potential of the Env complex, and hence which cells the virus can infect. Binding to CCR5 involves a region adjacent in addition to V3.

    Keywords - Domaini

    Coiled coil, Signal, Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di2.170.40.20. 2 hits.
    InterProiIPR000777. HIV1_GP160.
    IPR000328. Retroviral_envelope_protein.
    [Graphical view]
    PfamiPF00516. GP120. 1 hit.
    PF00517. GP41. 1 hit.
    [Graphical view]
    SUPFAMiSSF56502. SSF56502. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P35961-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRATEIRKNY QHLWKGGTLL LGMLMICSAA EQLWVTVYYG VPVWKEATTT    50
    LFCASDAKAY DTEVHNVWAT HACVPTDPNP QEVKLENVTE NFNMWKNNMV 100
    EQMHEDIISL WDQSLKPCVK LTPLCVTLNC TDLRNATNTT SSSWETMEKG 150
    EIKNCSFNIT TSIRDKVQKE YALFYNLDVV PIDNASYRLI SCNTSVITQA 200
    CPKVSFEPIP IHYCAPAGFA ILKCNDKKFN GTGPCTNVST VQCTHGIRPV 250
    VSTQLLLNGS LAEEEIVIRS ENFTNNAKTI IVQLNESVVI NCTRPNNNTR 300
    KSINIGPGRA LYTTGEIIGD IRQAHCNLSK TQWENTLEQI AIKLKEQFGN 350
    NKTIIFNPSS GGDPEIVTHS FNCGGEFFYC NSTQLFTWND TRKLNNTGRN 400
    ITLPCRIKQI INMWQEVGKA MYAPPIRGQI RCSSNITGLL LTRDGGKDTN 450
    GTEIFRPGGG DMRDNWRSEL YKYKVVKIEP LGVAPTKAKR RVVQREKRAV 500
    GLGALFLGFL GAAGSTMGAA SITLTVQARQ LLSGIVQQQN NLLRAIEAQQ 550
    HLLQLTVWGI KQLQARVLAV ERYLRDQQLL GIWGCSGKLI CTTTVPWNTS 600
    WSNKSLNEIW DNMTWMKWER EIDNYTHIIY SLIEQSQNQQ EKNEQELLAL 650
    DKWASLWNWF DITKWLWYIK IFIMIVGGLI GLRIVFVVLS IVNRVRQGYS 700
    PLSFQTHLPA QRGPDRPDGI EEEGGERDRD RSGPLVDGFL AIIWVDLRSL 750
    CLFSYHRLRD LLLIVTRIVE LLGRRGWGVL KYWWNLLQYW IQELKNSAVS 800
    LLNATAIAVA EGTDRVIEIL QRAFRAVLHI PVRIRQGLER ALL 843
    Length:843
    Mass (Da):95,648
    Last modified:June 1, 1994 - v1
    Checksum:iC69DFD971C918B71
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93258 Genomic RNA. No translation available.
    PIRiH44001.

    Cross-referencesi

    Web resourcesi

    hivdb

    HIV drug resistance database

    BioAfrica: HIV bioinformatics in Africa
    HIV drug resistance mutations

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93258 Genomic RNA. No translation available.
    PIRi H44001.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G9N X-ray 2.90 G 82-479 [» ]
    1RZK X-ray 2.90 G 82-479 [» ]
    1YYL X-ray 2.75 G/P 82-479 [» ]
    1YYM X-ray 2.20 G/P 82-479 [» ]
    2I5Y X-ray 2.20 G/P 82-479 [» ]
    2I60 X-ray 2.40 G/P 82-479 [» ]
    2NY7 X-ray 2.30 G 158-479 [» ]
    2QAD X-ray 3.30 A/E 88-479 [» ]
    3HI1 X-ray 2.90 G/J 89-479 [» ]
    3TGQ X-ray 3.40 A/B/C/D 43-479 [» ]
    4DVR X-ray 2.50 G 82-479 [» ]
    4JO3 X-ray 2.60 P/Q 313-327 [» ]
    4JZW X-ray 1.78 A/G 43-479 [» ]
    4JZZ X-ray 1.49 A 43-479 [» ]
    4K0A X-ray 2.13 A 43-479 [» ]
    4KA2 X-ray 1.79 A 43-479 [» ]
    4LAJ X-ray 2.14 A/B/F/J 43-479 [» ]
    ProteinModelPortali P35961.
    SMRi P35961. Positions 89-122, 195-479, 499-652.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48439N.

    Chemistry

    BindingDBi P35961.
    ChEMBLi CHEMBL6180.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P35961.

    Family and domain databases

    Gene3Di 2.170.40.20. 2 hits.
    InterProi IPR000777. HIV1_GP160.
    IPR000328. Retroviral_envelope_protein.
    [Graphical view ]
    Pfami PF00516. GP120. 1 hit.
    PF00517. GP41. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56502. SSF56502. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence, genome organization, and biological properties of human immunodeficiency virus type 1 in vivo: evidence for limited defectiveness and complementation."
      Li Y., Hui H., Burgess C.J., Price R.W., Sharp P.M., Hahn B.H., Shaw G.M.
      J. Virol. 66:6587-6600(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding."
      Rizzuto C.D., Wyatt R., Hernandez-Ramos N., Sun Y., Kwong P.D., Hendrickson W.A., Sodroski J.
      Science 280:1949-1953(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION OF SURFACE PROTEIN GP120 WITH HUMAN CCR5.
    3. "Pathogens target DC-SIGN to influence their fate DC-SIGN functions as a pathogen receptor with broad specificity."
      Geijtenbeek T.B., van Kooyk Y.
      APMIS 111:698-714(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    4. Cited for: REVIEW.
    5. Cited for: REVIEW.
    6. Cited for: REVIEW.
    7. "Emerging drug targets for antiretroviral therapy."
      Reeves J.D., Piefer A.J.
      Drugs 65:1747-1766(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    8. "HIV and the chemokine system: 10 years later."
      Lusso P.
      EMBO J. 25:447-456(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiENV_HV1Y2
    AccessioniPrimary (citable) accession number: P35961
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Inhibitors targeting HIV-1 viral envelope proteins are used as antiretroviral drugs. Attachment of virions to the cell surface via non-specific interactions and CD4 binding can be blocked by inhibitors that include cyanovirin-N, cyclotriazadisulfonamide analogs, PRO 2000, TNX 355 and PRO 542. In addition, BMS 806 can block CD4-induced conformational changes. Env interactions with the coreceptor molecules can be targeted by CCR5 antagonists including SCH-D, maraviroc (UK 427857) and aplaviroc (GW 873140), and the CXCR4 antagonist AMD 070. Fusion of viral and cellular membranes can be inhibited by peptides such as enfuvirtide and tifuvirtide (T 1249). Resistance to inhibitors associated with mutations in Env are observed. 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.
    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).

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

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