#ID(s) interactor A	ID(s) interactor B	Alt. ID(s) interactor A	Alt. ID(s) interactor B	Alias(es) interactor A	Alias(es) interactor B	Interaction detection method(s)	Publication 1st author(s)	Publication Identifier(s)	Taxid interactor A	Taxid interactor B	Interaction type(s)	Source database(s)	Interaction identifier(s)	Confidence value(s)	Expansion method(s)	Biological role(s) interactor A	Biological role(s) interactor B	Experimental role(s) interactor A	Experimental role(s) interactor B	Type(s) interactor A	Type(s) interactor B	Xref(s) interactor A	Xref(s) interactor B	Interaction Xref(s)	Annotation(s) interactor A	Annotation(s) interactor B	Interaction annotation(s)	Host organism(s)	Interaction parameter(s)	Creation date	Update date	Checksum(s) interactor A	Checksum(s) interactor B	Interaction Checksum(s)	Negative	Feature(s) interactor A	Feature(s) interactor B	Stoichiometry(s) interactor A	Stoichiometry(s) interactor B	Identification method participant A	Identification method participant B
uniprotkb:P04580	uniprotkb:P03375	intact:EBI-8629112|intact:MINT-1523040	intact:EBI-8629151|uniprotkb:P03376|intact:MINT-1523031|psi-mi:MINT-5262998	psi-mi:env_hv1z6(display_long)|uniprotkb:env(gene name)|psi-mi:env(display_short)|uniprotkb:Env polyprotein(gene name synonym)	psi-mi:env_hv1b1(display_long)|uniprotkb:env(gene name)|psi-mi:env(display_short)|uniprotkb:Env polyprotein(gene name synonym)	psi-mi:"MI:0114"(x-ray crystallography)	Chan et al. (1997)	mint:MINT-5221431|pubmed:9108481	taxid:11708(hv1z6)|taxid:11708("Human immunodeficiency virus type 1 group M subtype D (isolate Z6)")	taxid:11678(hv1b1)|taxid:11678("Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1)")	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-8629145|mint:MINT-24869	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	go:"GO:0005198"(structural molecule activity)|go:"GO:0016021"(integral component of membrane)|go:"GO:0019031"(viral envelope)|go:"GO:0019062"(virion attachment to host cell)|go:"GO:0019064"(fusion of virus membrane with host plasma membrane)|go:"GO:0019082"(viral protein processing)|go:"GO:0020002"(host cell plasma membrane)|go:"GO:0030683"(mitigation of host immune response by virus)|go:"GO:0039654"(fusion of virus membrane with host endosome membrane)|go:"GO:0044175"(host cell endosome membrane)|go:"GO:0044423"(virion component)|go:"GO:0055036"(virion membrane)|go:"GO:0075512"(clathrin-dependent endocytosis of virus by host cell)|go:"GO:0090527"(actin filament reorganization)|go:"GO:1903905"(positive regulation of establishment of T cell polarity)|go:"GO:1903908"(positive regulation of plasma membrane raft polarization)|go:"GO:1903911"(positive regulation of receptor clustering)|rcsb pdb:1TJH|rcsb pdb:3G7A|rcsb pdb:1TJI|rcsb pdb:3F50|rcsb pdb:3F4Y|interpro:IPR037527|rcsb pdb:3MOD|rcsb pdb:4I2L|rcsb pdb:3MOA|rcsb pdb:3MOB|reactome:R-HSA-5621480|interpro:IPR036377|interpro:IPR000328(Envelope Polyprotein GP41)|interpro:IPR000777(Envelope glycoprotein GP120)|mint:MINT-1523054(identity)	go:"GO:0005198"(structural molecule activity)|go:"GO:0016021"(integral component of membrane)|go:"GO:0019031"(viral envelope)|rcsb pdb:3W19|go:"GO:0019064"(fusion of virus membrane with host plasma membrane)|go:"GO:0019082"(viral protein processing)|go:"GO:0020002"(host cell plasma membrane)|go:"GO:0030683"(mitigation of host immune response by virus)|go:"GO:0039654"(fusion of virus membrane with host endosome membrane)|go:"GO:0042609"(CD4 receptor binding)|go:"GO:0044175"(host cell endosome membrane)|go:"GO:0044220"(host cell perinuclear region of cytoplasm)|go:"GO:0044423"(virion component)|go:"GO:0044538"(host cell periphery)|go:"GO:0044877"(protein-containing complex binding)|go:"GO:0055036"(virion membrane)|go:"GO:0075512"(clathrin-dependent endocytosis of virus by host cell)|go:"GO:0090527"(actin filament reorganization)|go:"GO:1903905"(positive regulation of establishment of T cell polarity)|go:"GO:1903908"(positive regulation of plasma membrane raft polarization)|go:"GO:1903911"(positive regulation of receptor clustering)|go:"GO:0019062"(virion attachment to host cell)|rcsb pdb:3VU6|rcsb pdb:3VU5|rcsb pdb:3VH7|rcsb pdb:3VGY|rcsb pdb:2ARI|interpro:IPR037527|reactome:R-HSA-5621480|interpro:IPR036377|rcsb pdb:6ME1|interpro:IPR000328(Envelope Polyprotein GP41)|interpro:IPR000777(Envelope glycoprotein GP120)|mint:MINT-1523047(identity)	-	comment:mint|function:"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. Fusion occurs at the host cell plasma membrane"|function:"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 viral and target cell membrane fusion, 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. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm"|function:"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"|function: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|function:"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"|function:"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"|comment:"Stoichiometry: 1.0"	comment:mint|comment:"Stoichiometry: 1.0"	comment:In the xray complex 1aik, P03376 is chain C and P04580 is chain N Resolution 2.000|comment:homomint|comment:mint|dataset:Virus - Publications including interactions involving viral proteins	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2004/02/12	2014/10/16	rogid:q1pL1myY1oLkZhUrg2lDntKu8FE11708	rogid:nL/te1Y8ZmTrAZeEjzV/IBT1wIE11678	intact-crc:4439DFD8BEE09E2C|rigid:b/dkl6cq9Gx3doVf/97dHV6cB6Y	false	tag:?-?(MINT-1523055)	tag:?-?(MINT-1523048)	1	1	psi-mi:"MI:0078"(nucleotide sequence identification)	psi-mi:"MI:0078"(nucleotide sequence identification)