9di2

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Current revision (05:33, 17 September 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9di2 is ON HOLD until 2026-09-17
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==Cryo-EM structure of the USP1-UAF1-Ubiquitin-VS complex==
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<StructureSection load='9di2' size='340' side='right'caption='[[9di2]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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Authors: Griffith, J.P.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9di2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9DI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9DI2 FirstGlance]. <br>
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Description: Cryo-EM structure of the USP1-UAF1-Ubiquitin-VS complex
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1A4Y:3-methylsulfonylpropan-1-amine'>A1A4Y</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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[[Category: Griffith, J.P]]
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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=9di2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9di2 OCA], [https://pdbe.org/9di2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9di2 RCSB], [https://www.ebi.ac.uk/pdbsum/9di2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9di2 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/WDR48_HUMAN WDR48_HUMAN] Autosomal recessive spastic paraplegia type 60.
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== Function ==
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[https://www.uniprot.org/uniprot/WDR48_HUMAN WDR48_HUMAN] Regulator of deubiquitinating complexes. Acts as a strong activator of USP1 by enhancing the USP1-mediated deubiquitination of FANCD2; USP1 being almost inactive by itself. Also activates deubiquitinating activity of complexes containing USP12 and USP46, respectively. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate. In case of infection by Herpesvirus saimiri, may play a role in vesicular transport or membrane fusion events necessary for transport to lysosomes. Induces lysosomal vesicle formation via interaction with Herpesvirus saimiri tyrosine kinase-interacting protein (TIP). Subsequently, TIP recruits tyrosine-protein kinase LCK, resulting in down-regulation of T-cell antigen receptor TCR. May play a role in generation of enlarged endosomal vesicles via interaction with TIP. In case of infection by papillomavirus HPV11, promotes the maintenance of the viral genome via its interaction with HPV11 helicase E1.<ref>PMID:12196293</ref> <ref>PMID:18082604</ref> <ref>PMID:19075014</ref>
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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: Griffith JP]]

Current revision

Cryo-EM structure of the USP1-UAF1-Ubiquitin-VS complex

PDB ID 9di2

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