2goh: Difference between revisions

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==Three-dimensional Structure of the Trans-membrane Domain of Vpu from HIV-1 in Aligned Phospholipid Bicelles==
==Three-dimensional Structure of the Trans-membrane Domain of Vpu from HIV-1 in Aligned Phospholipid Bicelles==
<StructureSection load='2goh' size='340' side='right'caption='[[2goh]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
<StructureSection load='2goh' size='340' side='right'caption='[[2goh]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2goh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/9hiv1 9hiv1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GOH FirstGlance]. <br>
<table><tr><td colspan='2'>[[2goh]] 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=2GOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GOH FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2gof|2gof]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VPU ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 9HIV1])</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=2goh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2goh OCA], [https://pdbe.org/2goh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2goh RCSB], [https://www.ebi.ac.uk/pdbsum/2goh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2goh 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=2goh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2goh OCA], [https://pdbe.org/2goh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2goh RCSB], [https://www.ebi.ac.uk/pdbsum/2goh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2goh 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).  
[https://www.uniprot.org/uniprot/Q2NN19_9HIV1 Q2NN19_9HIV1] Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor 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 promote 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.[HAMAP-Rule:MF_04082][RuleBase:RU364058]
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human immunodeficiency virus 1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Angelis, A A.De]]
[[Category: De Angelis AA]]
[[Category: Nevzorov, A A]]
[[Category: Nevzorov AA]]
[[Category: Opella, S J]]
[[Category: Opella SJ]]
[[Category: Park, S H]]
[[Category: Park SH]]
[[Category: Wu, C H]]
[[Category: Wu CH]]
[[Category: 16c bicelle]]
[[Category: Magnetic alignment]]
[[Category: Trans-membrane helix]]
[[Category: Viral protein]]

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