8sh9
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==CCT G beta 5 complex best PhLP1 class== | |
| - | + | <StructureSection load='8sh9' size='340' side='right'caption='[[8sh9]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8sh9]] is a 18 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=8SH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SH9 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]] 2.7Å</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>, <scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | [[Category: Sass | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8sh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sh9 OCA], [https://pdbe.org/8sh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sh9 RCSB], [https://www.ebi.ac.uk/pdbsum/8sh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sh9 ProSAT]</span></td></tr> |
| - | [[Category: Shen | + | </table> |
| - | [[Category: Wang | + | == Function == |
| - | [[Category: Willardson | + | [https://www.uniprot.org/uniprot/TCPD_HUMAN TCPD_HUMAN] Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Sass M]] | ||
| + | [[Category: Shen PS]] | ||
| + | [[Category: Wang S]] | ||
| + | [[Category: Willardson BM]] | ||
Revision as of 07:08, 25 October 2023
CCT G beta 5 complex best PhLP1 class
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