8sgl
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 8sgl is ON HOLD Authors: Wang, S., Sass, M., Willardson, B.M., Shen, P.S. Description: CCT G beta 5 complex closed state 15 [[Category: Unreleased ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==CCT G beta 5 complex closed state 15== | |
| + | <StructureSection load='8sgl' size='340' side='right'caption='[[8sgl]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8sgl]] is a 17 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=8SGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SGL 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]] 2.9Å</td></tr> | ||
| + | <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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8sgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sgl OCA], [https://pdbe.org/8sgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sgl RCSB], [https://www.ebi.ac.uk/pdbsum/8sgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sgl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/TCPE_HUMAN TCPE_HUMAN] Hereditary sensory and autonomic neuropathy with spastic paraplegia. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TCPE_HUMAN TCPE_HUMAN] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin.<ref>PMID:20080638</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Transducin 3D structures|Transducin 3D structures]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Sass | + | __TOC__ |
| - | [[Category: Shen | + | </StructureSection> |
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| + | [[Category: Sass M]] | ||
| + | [[Category: Shen PS]] | ||
| + | [[Category: Wang S]] | ||
| + | [[Category: Willardson BM]] | ||
Current revision
CCT G beta 5 complex closed state 15
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