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| <SX load='6qb8' size='340' side='right' viewer='molstar' caption='[[6qb8]], [[Resolution|resolution]] 3.97Å' scene=''> | | <SX load='6qb8' size='340' side='right' viewer='molstar' caption='[[6qb8]], [[Resolution|resolution]] 3.97Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6qb8]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QB8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QB8 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6qb8]] 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=6QB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QB8 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></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]] 3.97Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TCP1, CCT1, CCTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CCT2, 99D8.1, CCTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CCT4, CCTD, SRB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CCT5, CCTE, KIAA0098 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CCT3, CCTG, TRIC5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CCT7, CCTH, NIP7-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CCT8, C21orf112, CCTQ, KIAA0002 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CCT6A, CCT6, CCTZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[http://proteopedia.org/fgij/fg.htm?mol=6qb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qb8 OCA], [http://pdbe.org/6qb8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qb8 RCSB], [http://www.ebi.ac.uk/pdbsum/6qb8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qb8 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=6qb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qb8 OCA], [https://pdbe.org/6qb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qb8 RCSB], [https://www.ebi.ac.uk/pdbsum/6qb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qb8 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Disease ==
| |
| [[http://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 == | | == Function == |
| [[http://www.uniprot.org/uniprot/TCPH_HUMAN TCPH_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).<ref>PMID:25467444</ref> [[http://www.uniprot.org/uniprot/TCPD_HUMAN TCPD_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). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref> [[http://www.uniprot.org/uniprot/TCPQ_HUMAN TCPQ_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). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref> [[http://www.uniprot.org/uniprot/TCPB_HUMAN TCPB_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). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref> [[http://www.uniprot.org/uniprot/TCPZ_HUMAN 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).<ref>PMID:25467444</ref> [[http://www.uniprot.org/uniprot/TCPA_HUMAN TCPA_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). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref> [[http://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> [[http://www.uniprot.org/uniprot/TCPG_HUMAN TCPG_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). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref> | | [https://www.uniprot.org/uniprot/TCPB_HUMAN TCPB_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). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </div> | | </div> |
| <div class="pdbe-citations 6qb8" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6qb8" style="background-color:#fffaf0;"></div> |
| | |
| | ==See Also== |
| | *[[Chaperonin 3D structures|Chaperonin 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Bueno-Carrasco, M T]] | | [[Category: Bueno-Carrasco MT]] |
| [[Category: Cuellar, J]] | | [[Category: Cuellar J]] |
| [[Category: Ludlam, W G]] | | [[Category: Ludlam WG]] |
| [[Category: Santiago, C]] | | [[Category: Santiago C]] |
| [[Category: Valpuesta, J M]] | | [[Category: Valpuesta JM]] |
| [[Category: Willardson, B M]] | | [[Category: Willardson BM]] |
| [[Category: Cct]]
| |
| [[Category: Chaperone]]
| |
| [[Category: Folding]]
| |
| [[Category: Mlst8]]
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| [[Category: Wd40]]
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