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==Structure of the channel-forming trans-membrane domain of Virus protein "u" (Vpu) from HIV-1== | ==Structure of the channel-forming trans-membrane domain of Virus protein "u" (Vpu) from HIV-1== | ||
<StructureSection load='1pi8' size='340' side='right'caption='[[1pi8 | <StructureSection load='1pi8' size='340' side='right'caption='[[1pi8]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1pi8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1pi8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PI8 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pi8 OCA], [https://pdbe.org/1pi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pi8 RCSB], [https://www.ebi.ac.uk/pdbsum/1pi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pi8 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pi8 OCA], [https://pdbe.org/1pi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pi8 RCSB], [https://www.ebi.ac.uk/pdbsum/1pi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pi8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/VPU_HV1LW VPU_HV1LW] Enhances virion budding, by targeting human CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its receptor human CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to interfere with the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1pi8 ConSurf]. | </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=1pi8 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Vpu protein|Vpu protein]] | *[[Vpu protein|Vpu protein]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human immunodeficiency virus 1]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mesleh | [[Category: Mesleh MF]] | ||
[[Category: Montal | [[Category: Montal M]] | ||
[[Category: Mrse | [[Category: Mrse AA]] | ||
[[Category: Nevzorov | [[Category: Nevzorov AA]] | ||
[[Category: Oblatt-Montal | [[Category: Oblatt-Montal M]] | ||
[[Category: Opella | [[Category: Opella SJ]] | ||
[[Category: Park | [[Category: Park SH]] | ||
Revision as of 08:55, 17 April 2024
Structure of the channel-forming trans-membrane domain of Virus protein "u" (Vpu) from HIV-1Structure of the channel-forming trans-membrane domain of Virus protein "u" (Vpu) from HIV-1
Structural highlights
FunctionVPU_HV1LW Enhances virion budding, by targeting human CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its receptor human CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to interfere with the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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