1whg
From Proteopedia
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==Solution structure of the CAP-Gly domain in mouse tubulin specific chaperone B== | ==Solution structure of the CAP-Gly domain in mouse tubulin specific chaperone B== | ||
| - | <StructureSection load='1whg' size='340' side='right'caption='[[1whg | + | <StructureSection load='1whg' size='340' side='right'caption='[[1whg]]' 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/Mus_musculus Mus musculus]. 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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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> | ||
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| - | ==See Also== | ||
| - | *[[CAP-Gly domain|CAP-Gly domain]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: Inoue | + | [[Category: Inoue M]] |
| - | [[Category: Kigawa | + | [[Category: Kigawa T]] |
| - | [[Category: Koshiba | + | [[Category: Koshiba S]] |
| - | + | [[Category: Saito K]] | |
| - | [[Category: Saito | + | [[Category: Yokoyama S]] |
| - | [[Category: Yokoyama | + | |
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Current revision
Solution structure of the CAP-Gly domain in mouse tubulin specific chaperone B
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Categories: Large Structures | Mus musculus | Inoue M | Kigawa T | Koshiba S | Saito K | Yokoyama S
