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8i6j

From Proteopedia

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Current revision (11:42, 1 February 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8i6j is ON HOLD until Paper Publication
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==The focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in the open state==
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<StructureSection load='8i6j' size='340' side='right'caption='[[8i6j]], [[Resolution|resolution]] 3.82&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8i6j]] is a 2 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=8I6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8I6J FirstGlance]. <br>
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Description:
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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]] 3.82&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=8i6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i6j OCA], [https://pdbe.org/8i6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i6j RCSB], [https://www.ebi.ac.uk/pdbsum/8i6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i6j ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PDCL3_HUMAN PDCL3_HUMAN] Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (PubMed:23792958, PubMed:26059764). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (PubMed:17429077). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (PubMed:15371430).[UniProtKB:Q4KLJ8]<ref>PMID:15371430</ref> <ref>PMID:17429077</ref> <ref>PMID:23792958</ref> <ref>PMID:26059764</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: Kim H]]
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[[Category: Lim S]]
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[[Category: Park J]]
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[[Category: Roh SH]]

Current revision

The focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in the open state

PDB ID 8i6j

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