5uyz

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'''Unreleased structure'''
 
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The entry 5uyz is ON HOLD
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==Structure of Human T-complex protein 1 subunit epsilon (CCT5) mutant His147Arg==
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<StructureSection load='5uyz' size='340' side='right'caption='[[5uyz]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5uyz]] is a 4 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=5UYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UYZ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5uyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uyz OCA], [https://pdbe.org/5uyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uyz RCSB], [https://www.ebi.ac.uk/pdbsum/5uyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uyz ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[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.
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The human chaperonin TRiC consists of eight non-identical subunits, and its protein-folding activity is critical for cellular health. Misfolded proteins are associated with many human diseases, such as amyloid diseases, cancer, and neuropathies, making TRiC a potential therapeutic target. A detailed structural understanding of its ATP-dependent folding mechanism and substrate recognition is therefore of great importance. Of particular health-related interest is the mutation Histidine 147 to Arginine (H147R) in human TRiC subunit 5 (CCT5), which has been associated with hereditary sensory neuropathy. In this paper, we describe the crystal structures of CCT5 and the CCT5-H147R mutant, which provide important structural information for this vital protein-folding machine in humans. This first X-ray crystallographic study of a single human CCT subunit in the context of a hexadecameric complex can be expanded in the future to the other 7 subunits that form the TRiC complex.
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Authors:
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Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.,Pereira JH, McAndrew RP, Sergeeva OA, Ralston CY, King JA, Adams PD Sci Rep. 2017 Jun 16;7(1):3673. doi: 10.1038/s41598-017-03825-3. PMID:28623285<ref>PMID:28623285</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5uyz" style="background-color:#fffaf0;"></div>
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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: Adams PD]]
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[[Category: King JA]]
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[[Category: McAndrew RP]]
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[[Category: Pereira JH]]
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[[Category: Ralston CY]]
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[[Category: Sergeeva OA]]

Current revision

Structure of Human T-complex protein 1 subunit epsilon (CCT5) mutant His147Arg

PDB ID 5uyz

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