7lum: Difference between revisions

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====
==Human TRiC in ATP/AlFx closed state==
<StructureSection load='7lum' size='340' side='right'caption='[[7lum]]' scene=''>
<StructureSection load='7lum' size='340' side='right'caption='[[7lum]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
<table><tr><td colspan='2'>[[7lum]] is a 16 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=7LUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LUM FirstGlance]. <br>
</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=7lum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lum OCA], [https://pdbe.org/7lum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lum RCSB], [https://www.ebi.ac.uk/pdbsum/7lum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lum ProSAT]</span></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]] 4.5&#8491;</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=7lum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lum OCA], [https://pdbe.org/7lum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lum RCSB], [https://www.ebi.ac.uk/pdbsum/7lum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lum ProSAT]</span></td></tr>
</table>
</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==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Z-disk]]
[[Category: Aebersold R]]
[[Category: Chiu W]]
[[Category: Dermody TS]]
[[Category: Frydman J]]
[[Category: Gestaut D]]
[[Category: Knowlton JJ]]
[[Category: Leitner A]]
[[Category: Ma B]]
[[Category: Prasad BVV]]
[[Category: Seven AB]]
[[Category: Shanker S]]
[[Category: Taylor G]]
[[Category: Wilson GJ]]
[[Category: Yates NA]]

Latest revision as of 18:00, 6 March 2024

Human TRiC in ATP/AlFx closed stateHuman TRiC in ATP/AlFx closed state

Structural highlights

7lum is a 16 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 4.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

TCPE_HUMAN Hereditary sensory and autonomic neuropathy with spastic paraplegia. The disease is caused by mutations affecting the gene represented in this entry.

Function

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.[1]

See Also

References

  1. Seo S, Baye LM, Schulz NP, Beck JS, Zhang Q, Slusarski DC, Sheffield VC. BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly. Proc Natl Acad Sci U S A. 2010 Jan 4. PMID:20080638 doi:http://dx.doi.org/0910268107

7lum, resolution 4.50Å

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OCA