1avz

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==V-1 NEF PROTEIN IN COMPLEX WITH WILD TYPE FYN SH3 DOMAIN==
==V-1 NEF PROTEIN IN COMPLEX WITH WILD TYPE FYN SH3 DOMAIN==
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<StructureSection load='1avz' size='340' side='right' caption='[[1avz]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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<StructureSection load='1avz' size='340' side='right'caption='[[1avz]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1avz]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AVZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1avz]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AVZ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HIV-1 NEF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1]), FYN TYROSINE KINASE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1avz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1avz OCA], [https://pdbe.org/1avz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1avz RCSB], [https://www.ebi.ac.uk/pdbsum/1avz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1avz ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1avz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1avz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1avz RCSB], [http://www.ebi.ac.uk/pdbsum/1avz PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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[https://www.uniprot.org/uniprot/NEF_HV1BR NEF_HV1BR] Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocytes function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. One of the earliest and most abundantly expressed viral proteins (By similarity).<ref>PMID:8151761</ref> <ref>PMID:8124721</ref> <ref>PMID:10684310</ref> <ref>PMID:11070003</ref> <ref>PMID:11285224</ref> <ref>PMID:11298454</ref> <ref>PMID:11861836</ref> <ref>PMID:14617802</ref> <ref>PMID:15854903</ref> <ref>PMID:16928758</ref> <ref>PMID:18005690</ref> In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection).<ref>PMID:8151761</ref> <ref>PMID:8124721</ref> <ref>PMID:10684310</ref> <ref>PMID:11070003</ref> <ref>PMID:11285224</ref> <ref>PMID:11298454</ref> <ref>PMID:11861836</ref> <ref>PMID:14617802</ref> <ref>PMID:15854903</ref> <ref>PMID:16928758</ref> <ref>PMID:18005690</ref> Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis (By similarity).<ref>PMID:8151761</ref> <ref>PMID:8124721</ref> <ref>PMID:10684310</ref> <ref>PMID:11070003</ref> <ref>PMID:11285224</ref> <ref>PMID:11298454</ref> <ref>PMID:11861836</ref> <ref>PMID:14617802</ref> <ref>PMID:15854903</ref> <ref>PMID:16928758</ref> <ref>PMID:18005690</ref> Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5. Interacts and decreases the half-life of p53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of Bad (By similarity).<ref>PMID:8151761</ref> <ref>PMID:8124721</ref> <ref>PMID:10684310</ref> <ref>PMID:11070003</ref> <ref>PMID:11285224</ref> <ref>PMID:11298454</ref> <ref>PMID:11861836</ref> <ref>PMID:14617802</ref> <ref>PMID:15854903</ref> <ref>PMID:16928758</ref> <ref>PMID:18005690</ref> Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors (By similarity).<ref>PMID:8151761</ref> <ref>PMID:8124721</ref> <ref>PMID:10684310</ref> <ref>PMID:11070003</ref> <ref>PMID:11285224</ref> <ref>PMID:11298454</ref> <ref>PMID:11861836</ref> <ref>PMID:14617802</ref> <ref>PMID:15854903</ref> <ref>PMID:16928758</ref> <ref>PMID:18005690</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/av/1avz_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/av/1avz_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1avz ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 1avz" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Tyrosine kinase|Tyrosine kinase]]
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*[[Protein Nef 3D structures|Protein Nef 3D structures]]
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*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
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[[Category: Transferase]]
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[[Category: Large Structures]]
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[[Category: Arold, S.]]
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[[Category: Arold S]]
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[[Category: Dumas, C.]]
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[[Category: Dumas C]]
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[[Category: Franken, P.]]
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[[Category: Franken P]]
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[[Category: Fyn]]
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[[Category: Gtp-binding]]
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[[Category: Hiv-1]]
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[[Category: Nef]]
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[[Category: Phosphorylation]]
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[[Category: Sh3 domain]]
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[[Category: Tyrosine kinase]]
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Current revision

V-1 NEF PROTEIN IN COMPLEX WITH WILD TYPE FYN SH3 DOMAIN

PDB ID 1avz

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