1vpu

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{{Seed}}
 
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[[Image:1vpu.png|left|200px]]
 
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==NMR SOLUTION STRUCTURE OF THE HIV-1 VPU CYTOPLASMIC DOMAIN, 9 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1vpu", creates the "Structure Box" on the page.
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<StructureSection load='1vpu' size='340' side='right'caption='[[1vpu]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1vpu]] 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=1VPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VPU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1vpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vpu OCA], [https://pdbe.org/1vpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vpu RCSB], [https://www.ebi.ac.uk/pdbsum/1vpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vpu ProSAT]</span></td></tr>
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{{STRUCTURE_1vpu| PDB=1vpu | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VPU_HV1S1 VPU_HV1S1] 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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vp/1vpu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</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/main_output.php?pdb_ID=1vpu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The human immunodeficiency virus type 1 Vpu protein enhances virus particle release from infected cells, decreases the tendency of syncytia formation and induces degradation of human CD4 receptor. It is known that the cytoplasmic part of Vpu is responsible for direct interaction to and degradation of CD4. The tertiary fold of the Vpu cytoplasmic domain in aqueous solution was determined employing NMR spectroscopy and molecular-dynamics simulated-annealing protocols. We found a very well defined amphipathic alpha-helix in the membrane proximal part (40-50), a less well defined helix (60-68), and a short alpha-helix at the C-terminus (75-79). We further determined the overall tertiary structure based on long-range nuclear Overhauser enhancement effects. Correlation of results from mutation experiments of Vpu and the structure data is discussed.
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===NMR SOLUTION STRUCTURE OF THE HIV-1 VPU CYTOPLASMIC DOMAIN, 9 STRUCTURES===
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Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution.,Willbold D, Hoffmann S, Rosch P Eur J Biochem. 1997 May 1;245(3):581-8. PMID:9182993<ref>PMID:9182993</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1vpu" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_9182993}}, adds the Publication Abstract to the page
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*[[Vpu protein|Vpu protein]]
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(as it appears on PubMed at http://www.pubmed.gov), where 9182993 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9182993}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human immunodeficiency virus 1]]
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1VPU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(isolate_12) Human immunodeficiency virus type 1 (isolate 12)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VPU OCA].
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[[Category: Large Structures]]
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[[Category: Hoffmann S]]
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==Reference==
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[[Category: Rosch P]]
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Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution., Willbold D, Hoffmann S, Rosch P, Eur J Biochem. 1997 May 1;245(3):581-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9182993 9182993]
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[[Category: Willbold D]]
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[[Category: Single protein]]
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[[Category: Hoffmann, S.]]
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[[Category: Rosch, P.]]
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[[Category: Willbold, D.]]
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[[Category: Aid]]
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[[Category: Hiv]]
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[[Category: Vpu]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:00:44 2008''
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Current revision

NMR SOLUTION STRUCTURE OF THE HIV-1 VPU CYTOPLASMIC DOMAIN, 9 STRUCTURES

PDB ID 1vpu

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