5uyx: Difference between revisions

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~~'''Unreleased structure'''~~

The entry ~~5uyx~~ is ~~ON HOLD~~

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

== Structural highlights ==

<table><tr><td colspan='2'>[[5uyx]] 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=5UYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UYX FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</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></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=5uyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uyx OCA], [https://pdbe.org/5uyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uyx RCSB], [https://www.ebi.ac.uk/pdbsum/5uyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uyx 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>

== Publication Abstract from PubMed ==

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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Adams PD]]

[[Category: King JA]]

[[Category: McAndrew RP]]

[[Category: Pereira JH]]

[[Category: Ralston CY]]

[[Category: Sergeeva OA]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5uyx is ON HOLD
+==Structure of Human T-complex protein 1 subunit epsilon (CCT5)==
+<StructureSection load='5uyx' size='340' side='right'caption='[[5uyx]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5uyx]] 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=5UYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UYX FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</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></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=5uyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uyx OCA], [https://pdbe.org/5uyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uyx RCSB], [https://www.ebi.ac.uk/pdbsum/5uyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uyx 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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5uyx" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Adams PD]]
+[[Category: King JA]]
+[[Category: McAndrew RP]]
+[[Category: Pereira JH]]
+[[Category: Ralston CY]]
+[[Category: Sergeeva OA]]