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P03377

- ENV_HV1BR

UniProt

P03377 - ENV_HV1BR

Protein

Envelope glycoprotein gp160

Gene

env

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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.1 Publication
    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
    Sitei516 – 5172Cleavage; by host furin

    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 BRU/LAI) (HIV-1)
    Taxonomic identifieri11686 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007692: 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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi184 – 1852LD → AA: Partial loss of CD4-independent binding. 1 Publication
    Mutagenesisi769 – 7691C → F: Almost no effect on virions assembly and infectivity. 2 Publications

    Keywords - Diseasei

    AIDS

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232By similarityAdd
    BLAST
    Chaini33 – 861829Envelope glycoprotein gp160PRO_0000239474Add
    BLAST
    Chaini33 – 516484Surface protein gp120PRO_0000038388Add
    BLAST
    Chaini517 – 861345Transmembrane protein gp41PRO_0000038389Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 741 Publication
    Glycosylationi88 – 881N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi119 ↔ 2101 Publication
    Disulfide bondi126 ↔ 2011 Publication
    Disulfide bondi131 ↔ 1621 Publication
    Glycosylationi136 – 1361N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi141 – 1411N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi146 – 1461N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi161 – 1611N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi165 – 1651N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi191 – 1911N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi202 – 2021N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi223 ↔ 2521 Publication
    Disulfide bondi233 ↔ 2441 Publication
    Glycosylationi235 – 2351N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi239 – 2391N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi246 – 2461N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi267 – 2671N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi281 – 2811N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi294 – 2941N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi300 – 3001N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi301 ↔ 3361 Publication
    Glycosylationi306 – 3061N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi337 – 3371N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi344 – 3441N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi361 – 3611N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi383 ↔ 4501 Publication
    Disulfide bondi390 ↔ 4231 Publication
    Glycosylationi391 – 3911N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi397 – 3971N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi402 – 4021N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi411 – 4111N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi453 – 4531N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi468 – 4681N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi603 ↔ 6091 Publication
    Glycosylationi616 – 6161N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi621 – 6211N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi630 – 6301N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi642 – 6421N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi679 – 6791N-linked (GlcNAc...); by hostSequence Analysis
    Lipidationi769 – 7691S-palmitoyl cysteine; by hostBy similarity
    Lipidationi842 – 8421S-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.1 Publication

    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

    Structurei

    Secondary structure

    1
    861
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi311 – 3144
    Beta strandi322 – 3254
    Helixi559 – 59436
    Helixi633 – 65523
    Helixi659 – 67416

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ENVX-ray2.60A546-593[»]
    A633-670[»]
    1ERFinfrared-A517-539[»]
    1FAVX-ray3.00A546-595[»]
    C639-670[»]
    1P5Ainfrared-A517-539[»]
    1U6UNMR-A310-326[»]
    1U6VNMR-A310-326[»]
    2ZZOX-ray2.20C633-666[»]
    N551-586[»]
    3G9RX-ray2.00A/B/C/D/E/F667-689[»]
    3MNWX-ray2.20P657-676[»]
    3VGXX-ray1.74C558-595[»]
    D626-657[»]
    3VTPX-ray1.90C555-595[»]
    D631-666[»]
    ProteinModelPortaliP03377.
    SMRiP03377. Positions 84-133, 200-497, 537-670.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03377.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini33 – 689657ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini711 – 861151CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei690 – 71021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni131 – 16131V1Add
    BLAST
    Regioni162 – 20140V2Add
    BLAST
    Regioni301 – 33535V3Add
    BLAST
    Regioni369 – 37911CD4-binding loopBy similarityAdd
    BLAST
    Regioni390 – 42334V4Add
    BLAST
    Regioni466 – 47611V5Add
    BLAST
    Regioni517 – 53721Fusion peptideSequence AnalysisAdd
    BLAST
    Regioni581 – 59717ImmunosuppressionBy similarityAdd
    BLAST
    Regioni667 – 68822MPER; binding to GalCerBy similarityAdd
    BLAST
    Regioni667 – 6726Involved in GalCer bindingBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili638 – 67235Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi184 – 1863Putative binding site to alpha-4/beta-7 integrin
    Motifi717 – 7204YXXL motif; contains endocytosis signalBy similarity
    Motifi860 – 8612Di-leucine internalization motifBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi465 – 4684Poly-Asn

    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.

    Sequence similaritiesi

    Belongs to the lentiviruses env family.Curated

    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. 3 hits.

    Sequencei

    Sequence statusi: Complete.

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

    P03377-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRVKEKYQHL WRWGWKWGTM LLGILMICSA TEKLWVTVYY GVPVWKEATT    50
    TLFCASDAKA YDTEVHNVWA THACVPTDPN PQEVVLVNVT ENFNMWKNDM 100
    VEQMHEDIIS LWDQSLKPCV KLTPLCVSLK CTDLGNATNT NSSNTNSSSG 150
    EMMMEKGEIK NCSFNISTSI RGKVQKEYAF FYKLDIIPID NDTTSYTLTS 200
    CNTSVITQAC PKVSFEPIPI HYCAPAGFAI LKCNNKTFNG TGPCTNVSTV 250
    QCTHGIRPVV STQLLLNGSL AEEEVVIRSA NFTDNAKTII VQLNQSVEIN 300
    CTRPNNNTRK SIRIQRGPGR AFVTIGKIGN MRQAHCNISR AKWNATLKQI 350
    ASKLREQFGN NKTIIFKQSS GGDPEIVTHS FNCGGEFFYC NSTQLFNSTW 400
    FNSTWSTEGS NNTEGSDTIT LPCRIKQFIN MWQEVGKAMY APPISGQIRC 450
    SSNITGLLLT RDGGNNNNGS EIFRPGGGDM RDNWRSELYK YKVVKIEPLG 500
    VAPTKAKRRV VQREKRAVGI GALFLGFLGA AGSTMGARSM TLTVQARQLL 550
    SGIVQQQNNL LRAIEAQQHL LQLTVWGIKQ LQARILAVER YLKDQQLLGI 600
    WGCSGKLICT TAVPWNASWS NKSLEQIWNN MTWMEWDREI NNYTSLIHSL 650
    IEESQNQQEK NEQELLELDK WASLWNWFNI TNWLWYIKIF IMIVGGLVGL 700
    RIVFAVLSIV NRVRQGYSPL SFQTHLPTPR GPDRPEGIEE EGGERDRDRS 750
    IRLVNGSLAL IWDDLRSLCL FSYHRLRDLL LIVTRIVELL GRRGWEALKY 800
    WWNLLQYWSQ ELKNSAVSLL NATAIAVAEG TDRVIEVVQG ACRAIRHIPR 850
    RIRQGLERIL L 861
    Length:861
    Mass (Da):97,488
    Last modified:July 21, 1986 - v1
    Checksum:i04DE2B4D4E4FD63A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti135 – 1373GNA → KND in strain: Clone pNL4-3.
    Natural varianti143 – 1475Missing in strain: Clone pNL4-3.
    Natural varianti151 – 1533EMM → RMI in strain: Clone pNL4-3.
    Natural varianti172 – 1721G → D in strain: Clone pNL4-3.
    Natural varianti187 – 1871I → V in strain: Clone pNL4-3.
    Natural varianti192 – 1932Missing in strain: Clone pNL4-3.
    Natural varianti197 – 1993TLT → RLI in strain: Clone pNL4-3.
    Natural varianti274 – 2741E → D in strain: Clone pNL4-3.
    Natural varianti295 – 2951Q → T in strain: Clone pNL4-3.
    Natural varianti538 – 5381R → A in strain: Clone pNL4-3.
    Natural varianti552 – 5521G → D in strain: Clone pNL4-3.
    Natural varianti689 – 6891I → L in strain: Clone pNL4-3.
    Natural varianti728 – 7281T → I in strain: Clone pNL4-3.
    Natural varianti818 – 8181S → N in strain: Clone pNL4-3.
    Natural varianti838 – 8425VQGAC → LQAAY in strain: Clone pNL4-3.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02013 Genomic RNA. Translation: AAB59751.1.
    A04321 Unassigned RNA. Translation: CAA00352.1.
    M19921 Genomic RNA. Translation: AAA44992.2.
    PIRiA03975. VCLJLV.

    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
    K02013 Genomic RNA. Translation: AAB59751.1 .
    A04321 Unassigned RNA. Translation: CAA00352.1 .
    M19921 Genomic RNA. Translation: AAA44992.2 .
    PIRi A03975. VCLJLV.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ENV X-ray 2.60 A 546-593 [» ]
    A 633-670 [» ]
    1ERF infrared - A 517-539 [» ]
    1FAV X-ray 3.00 A 546-595 [» ]
    C 639-670 [» ]
    1P5A infrared - A 517-539 [» ]
    1U6U NMR - A 310-326 [» ]
    1U6V NMR - A 310-326 [» ]
    2ZZO X-ray 2.20 C 633-666 [» ]
    N 551-586 [» ]
    3G9R X-ray 2.00 A/B/C/D/E/F 667-689 [» ]
    3MNW X-ray 2.20 P 657-676 [» ]
    3VGX X-ray 1.74 C 558-595 [» ]
    D 626-657 [» ]
    3VTP X-ray 1.90 C 555-595 [» ]
    D 631-666 [» ]
    ProteinModelPortali P03377.
    SMRi P03377. Positions 84-133, 200-497, 537-670.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P03377.
    ChEMBLi CHEMBL5826.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P03377.

    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. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the AIDS virus, LAV."
      Wain-Hobson S., Sonigo P., Danos O., Cole S., Alizon M.
      Cell 40:9-17(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Buckler C.E.
      Submitted (JUL-1989) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Clone pNL4-3.
    3. Strebel K.J., Martin M.A.
      Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 537 AND 538.
    4. "Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp 120."
      Curtis B.M., Scharnowske S., Watson A.J.
      Proc. Natl. Acad. Sci. U.S.A. 89:8356-8360(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION OF SURFACE PROTEIN GP120 WITH HUMAN CD209/DC-SIGN.
    5. "DC-SIGN interactions with human immunodeficiency virus type 1 and 2 and simian immunodeficiency virus."
      Pohlmann S., Baribaud F., Lee B., Leslie G.J., Sanchez M.D., Hiebenthal-Millow K., Munch J., Kirchhoff F., Doms R.W.
      J. Virol. 75:4664-4672(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION OF SURFACE PROTEIN GP120 WITH HOST CD209/DC-SIGN.
      Strain: Clone pNL4-3.
    6. "DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection."
      Kwon D.S., Gregorio G., Bitton N., Hendrickson W.A., Littman D.R.
      Immunity 16:135-144(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION OF SURFACE PROTEIN GP120 WITH HUMAN CD209/DC-SIGN, ROLE IN TRANS INFECTION.
      Strain: Clone pNL4-3.
    7. "Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry."
      Gallina A., Hanley T.M., Mandel R., Trahey M., Broder C.C., Viglianti G.A., Ryser H.J.
      J. Biol. Chem. 277:50579-50588(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
    8. "Polyarginine inhibits gp160 processing by furin and suppresses productive human immunodeficiency virus type 1 infection."
      Kibler K.V., Miyazato A., Yedavalli V.S.R.K., Dayton A.I., Jacobs B.L., Dapolito G., Kim S.-J., Jeang K.-T.
      J. Biol. Chem. 279:49055-49063(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN BY HOST FURIN.
      Strain: Clone pNL4-3.
    9. "Human immunodeficiency virus type 1 envelope glycoproteins that lack cytoplasmic domain cysteines: impact on association with membrane lipid rafts and incorporation onto budding virus particles."
      Bhattacharya J., Peters P.J., Clapham P.R.
      J. Virol. 78:5500-5506(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE OF PALMITOYLATION, MUTAGENESIS OF CYS-769.
      Strain: Clone pNL4-3.
    10. "Role of protein disulfide isomerase and other thiol-reactive proteins in HIV-1 envelope protein-mediated fusion."
      Ou W., Silver J.
      Virology 350:406-417(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY HUMAN TXN.
      Strain: Clone pNL4-3.
    11. "Only five of 10 strictly conserved disulfide bonds are essential for folding and eight for function of the HIV-1 envelope glycoprotein."
      van Anken E., Sanders R.W., Liscaljet I.M., Land A., Bontjer I., Tillemans S., Nabatov A.A., Paxton W.A., Berkhout B., Braakman I.
      Mol. Biol. Cell 19:4298-4309(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    12. "HIV-1 envelope protein binds to and signals through integrin alpha4beta7, the gut mucosal homing receptor for peripheral T cells."
      Arthos J., Cicala C., Martinelli E., Macleod K., Van Ryk D., Wei D., Xiao Z., Veenstra T.D., Conrad T.P., Lempicki R.A., McLaughlin S., Pascuccio M., Gopaul R., McNally J., Cruz C.C., Censoplano N., Chung E., Reitano K.N.
      , Kottilil S., Goode D.J., Fauci A.S.
      Nat. Immunol. 9:301-309(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION OF GP120 WITH HUMAN ITGA4/ITGB7 HETERODIMER, MUTAGENESIS OF 184-LEU-ASP-185.
      Strain: Clone pNL4-3.
    13. "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.
    14. Cited for: REVIEW.
    15. Cited for: REVIEW.
    16. Cited for: REVIEW.
    17. "Emerging drug targets for antiretroviral therapy."
      Reeves J.D., Piefer A.J.
      Drugs 65:1747-1766(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    18. "HIV and the chemokine system: 10 years later."
      Lusso P.
      EMBO J. 25:447-456(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    19. "The structure of an HIV-1 specific cell entry inhibitor in complex with the HIV-1 gp41 trimeric core."
      Zhou G., Ferrer M., Chopra R., Kapoor T.M., Strassmaier T., Weissenhorn W., Skehel J.J., Oprian D., Schreiber S.L., Harrison S.C., Wiley D.C.
      Bioorg. Med. Chem. 8:2219-2227(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 537-670.
    20. "Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane environments using (13)C-enhanced Fourier transform infrared spectroscopy."
      Gordon L.M., Mobley P.W., Pilpa R., Sherman M.A., Waring A.J.
      Biochim. Biophys. Acta 1559:96-120(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY FTIR OF 517-539.
    21. "Conformational mapping of the N-terminal peptide of HIV-1 gp41 in lipid detergent and aqueous environments using 13C-enhanced Fourier transform infrared spectroscopy."
      Gordon L.M., Mobley P.W., Lee W., Eskandari S., Kaznessis Y.N., Sherman M.A., Waring A.J.
      Protein Sci. 13:1012-1030(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY FTIR OF 517-539.

    Entry informationi

    Entry nameiENV_HV1BR
    AccessioniPrimary (citable) accession number: P03377
    Secondary accession number(s): Q85582
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 124 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
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3