7upn

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'''Unreleased structure'''
 
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The entry 7upn is ON HOLD until Paper Publication
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==Maedi visna virus Vif in complex with CypA and E3 ubiquitin ligase==
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<StructureSection load='7upn' size='340' side='right'caption='[[7upn]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7upn]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Visna-maedi_virus Visna-maedi virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UPN FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7upn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7upn OCA], [https://pdbe.org/7upn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7upn RCSB], [https://www.ebi.ac.uk/pdbsum/7upn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7upn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Lentiviral Vif molecules target the host antiviral APOBEC3 proteins for destruction in cellular ubiquitin-proteasome pathways. Different lentiviral Vifs have evolved to use the same canonical E3 ubiquitin ligase complexes, along with distinct noncanonical host cofactors for their activities. Unlike primate lentiviral Vif, which recruits CBFbeta as the noncanonical cofactor, nonprimate lentiviral Vif proteins have developed different cofactor recruitment mechanisms. Maedi-visna virus (MVV) sequesters CypA as the noncanonical cofactor for the Vif-mediated ubiquitination of ovine APOBEC3s. Here, we report the cryo-electron microscopy structure of MVV Vif in complex with CypA and E3 ligase components. The structure, along with our biochemical and functional analysis, reveals both conserved and unique structural elements of MVV Vif and its common and distinct interaction modes with various cognate cellular proteins, providing a further understanding of the evolutionary relationship between lentiviral Vifs and the molecular mechanisms by which they capture different host cofactors for immune evasion activities.
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Authors:
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Structural basis for recruitment of host CypA and E3 ubiquitin ligase by maedi-visna virus Vif.,Hu Y, Gudnadottir RB, Knecht KM, Arizaga F, Jonsson SR, Xiong Y Sci Adv. 2023 Jan 13;9(2):eadd3422. doi: 10.1126/sciadv.add3422. Epub 2023 Jan , 13. PMID:36638173<ref>PMID:36638173</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 7upn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Visna-maedi virus]]
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[[Category: Hu Y]]
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[[Category: Xiong Y]]

Revision as of 06:30, 25 January 2023

Maedi visna virus Vif in complex with CypA and E3 ubiquitin ligase

PDB ID 7upn

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