1v6e
From Proteopedia
(Difference between revisions)
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<StructureSection load='1v6e' size='340' side='right'caption='[[1v6e]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1v6e' size='340' side='right'caption='[[1v6e]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1v6e]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1v6e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V6E FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RIKEN cDNA 2410007D12 ([ | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RIKEN cDNA 2410007D12 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v6e OCA], [https://pdbe.org/1v6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v6e RCSB], [https://www.ebi.ac.uk/pdbsum/1v6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v6e ProSAT], [https://www.topsan.org/Proteins/RSGI/1v6e TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/TBCB_MOUSE TBCB_MOUSE]] Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer (By similarity). Involved in regulation of tubulin heterodimer dissociation. May function as a negative regulator of axonal growth.<ref>PMID:17184771</ref> <ref>PMID:17217416</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 06:33, 10 November 2021
Solution Structure of a N-terminal Ubiquitin-like Domain in Mouse Tubulin-specific Chaperone B
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Categories: Large Structures | Lk3 transgenic mice | Inoue, M | Kigawa, T | Koshiba, S | Structural genomic | Saito, K | Yokoyama, S | Zhao, C | Cytoskeleton | Cytoskeleton-associated protein ckap1 | Microtubule | Rsgi | Structural protein | Tubulin folding cofactor b | Tubulin-specific chaperone b | Ubiquitin-like fold
