7x0s: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7x0s]] 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=7X0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7X0S FirstGlance]. <br>
<table><tr><td colspan='2'>[[7x0s]] 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=7X0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7X0S FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#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>, <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=7x0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7x0s OCA], [https://pdbe.org/7x0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7x0s RCSB], [https://www.ebi.ac.uk/pdbsum/7x0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7x0s ProSAT]</span></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=7x0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7x0s OCA], [https://pdbe.org/7x0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7x0s RCSB], [https://www.ebi.ac.uk/pdbsum/7x0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7x0s ProSAT]</span></td></tr>
</table>
</table>

Latest revision as of 08:51, 5 July 2023

Human TRiC-tubulin-S3Human TRiC-tubulin-S3

Structural highlights

7x0s is a 17 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.1Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TCPZ_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). The TRiC complex plays a role in the folding of actin and tubulin (Probable).[1]

References

  1. Freund A, Zhong FL, Venteicher AS, Meng Z, Veenstra TD, Frydman J, Artandi SE. Proteostatic control of telomerase function through TRiC-mediated folding of TCAB1. Cell. 2014 Dec 4;159(6):1389-403. doi: 10.1016/j.cell.2014.10.059. Epub 2014 Nov , 20. PMID:25467444 doi:http://dx.doi.org/10.1016/j.cell.2014.10.059

7x0s, resolution 3.10Å

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OCA