8i6j
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | '''Unreleased structure''' | ||
- | The | + | ==The focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in the open state== |
- | + | <StructureSection load='8i6j' size='340' side='right'caption='[[8i6j]], [[Resolution|resolution]] 3.82Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <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> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.82Å</td></tr> | |
- | [[Category: | + | <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> |
+ | <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> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [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> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Kim H]] | ||
+ | [[Category: Lim S]] | ||
+ | [[Category: Park J]] | ||
+ | [[Category: Roh SH]] |
Current revision
The focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in the open state
|
Categories: Homo sapiens | Large Structures | Kim H | Lim S | Park J | Roh SH