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P35961

- ENV_HV1Y2

UniProt

P35961 - ENV_HV1Y2

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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

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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 671640ExtracellularSequence AnalysisAdd
BLAST
Transmembranei672 – 69221HelicalSequence AnalysisAdd
BLAST
Topological domaini693 – 843151CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell endosome Source: UniProtKB-KW
  2. host cell plasma membrane Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
  4. viral envelope Source: UniProtKB-KW
Complete GO annotation...

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 – 554Combined sources
Beta strandi59 – 613Combined sources
Helixi64 – 729Combined sources
Beta strandi73 – 753Combined sources
Beta strandi82 – 843Combined sources
Beta strandi90 – 934Combined sources
Helixi94 – 963Combined sources
Helixi98 – 11417Combined sources
Beta strandi118 – 1225Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi211 – 2144Combined sources
Beta strandi219 – 2246Combined sources
Beta strandi231 – 24313Combined sources
Beta strandi252 – 2587Combined sources
Beta strandi263 – 2653Combined sources
Beta strandi267 – 2693Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi280 – 29415Combined sources
Beta strandi298 – 3003Combined sources
Turni306 – 3083Combined sources
Beta strandi323 – 3297Combined sources
Helixi330 – 34819Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi353 – 3564Combined sources
Beta strandi359 – 3613Combined sources
Helixi364 – 3674Combined sources
Beta strandi369 – 3735Combined sources
Beta strandi376 – 3805Combined sources
Helixi383 – 3853Combined sources
Helixi388 – 3903Combined sources
Turni396 – 3983Combined sources
Beta strandi400 – 41213Combined sources
Beta strandi414 – 4218Combined sources
Beta strandi426 – 4294Combined sources
Beta strandi430 – 44314Combined sources
Beta strandi446 – 4494Combined sources
Beta strandi452 – 4576Combined sources
Helixi462 – 4709Combined sources
Beta strandi473 – 4775Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4R4FX-ray3.51A43-479[»]
ProteinModelPortaliP35961.
SMRiP35961. Positions 89-122, 195-479, 499-652.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35961.

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

        10         20         30         40         50
MRATEIRKNY QHLWKGGTLL LGMLMICSAA EQLWVTVYYG VPVWKEATTT
60 70 80 90 100
LFCASDAKAY DTEVHNVWAT HACVPTDPNP QEVKLENVTE NFNMWKNNMV
110 120 130 140 150
EQMHEDIISL WDQSLKPCVK LTPLCVTLNC TDLRNATNTT SSSWETMEKG
160 170 180 190 200
EIKNCSFNIT TSIRDKVQKE YALFYNLDVV PIDNASYRLI SCNTSVITQA
210 220 230 240 250
CPKVSFEPIP IHYCAPAGFA ILKCNDKKFN GTGPCTNVST VQCTHGIRPV
260 270 280 290 300
VSTQLLLNGS LAEEEIVIRS ENFTNNAKTI IVQLNESVVI NCTRPNNNTR
310 320 330 340 350
KSINIGPGRA LYTTGEIIGD IRQAHCNLSK TQWENTLEQI AIKLKEQFGN
360 370 380 390 400
NKTIIFNPSS GGDPEIVTHS FNCGGEFFYC NSTQLFTWND TRKLNNTGRN
410 420 430 440 450
ITLPCRIKQI INMWQEVGKA MYAPPIRGQI RCSSNITGLL LTRDGGKDTN
460 470 480 490 500
GTEIFRPGGG DMRDNWRSEL YKYKVVKIEP LGVAPTKAKR RVVQREKRAV
510 520 530 540 550
GLGALFLGFL GAAGSTMGAA SITLTVQARQ LLSGIVQQQN NLLRAIEAQQ
560 570 580 590 600
HLLQLTVWGI KQLQARVLAV ERYLRDQQLL GIWGCSGKLI CTTTVPWNTS
610 620 630 640 650
WSNKSLNEIW DNMTWMKWER EIDNYTHIIY SLIEQSQNQQ EKNEQELLAL
660 670 680 690 700
DKWASLWNWF DITKWLWYIK IFIMIVGGLI GLRIVFVVLS IVNRVRQGYS
710 720 730 740 750
PLSFQTHLPA QRGPDRPDGI EEEGGERDRD RSGPLVDGFL AIIWVDLRSL
760 770 780 790 800
CLFSYHRLRD LLLIVTRIVE LLGRRGWGVL KYWWNLLQYW IQELKNSAVS
810 820 830 840
LLNATAIAVA EGTDRVIEIL QRAFRAVLHI PVRIRQGLER ALL
Length:843
Mass (Da):95,648
Last modified:June 1, 1994 - v1
Checksum:iC69DFD971C918B71
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
M93258 Genomic RNA. No translation available.
PIRi H44001.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 [» ]
4R4F X-ray 3.51 A 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: November 26, 2014
This is version 116 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

Dasty 3