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1whg
From Proteopedia
(Difference between revisions)
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<StructureSection load='1whg' size='340' side='right'caption='[[1whg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1whg' size='340' side='right'caption='[[1whg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1whg]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1whg]] 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=1WHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WHG 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=1whg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1whg OCA], [https://pdbe.org/1whg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1whg RCSB], [https://www.ebi.ac.uk/pdbsum/1whg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1whg ProSAT], [https://www.topsan.org/Proteins/RSGI/1whg 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]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1whg ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1whg ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | |||
| - | ==See Also== | ||
| - | *[[CAP-Gly domain|CAP-Gly domain]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 06:54, 2 March 2022
Solution structure of the CAP-Gly domain in mouse tubulin specific chaperone B
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