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4icv
From Proteopedia
(Difference between revisions)
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==Ubiquitin-like domain of human tubulin folding cofactor E - crystal form B== | ==Ubiquitin-like domain of human tubulin folding cofactor E - crystal form B== | ||
<StructureSection load='4icv' size='340' side='right' caption='[[4icv]], [[Resolution|resolution]] 1.45Å' scene=''> | <StructureSection load='4icv' size='340' side='right' caption='[[4icv]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4icu|4icu]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4icu|4icu]]</td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4icv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4icv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4icv RCSB], [http://www.ebi.ac.uk/pdbsum/4icv PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4icv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4icv OCA], [http://pdbe.org/4icv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4icv RCSB], [http://www.ebi.ac.uk/pdbsum/4icv PDBsum]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/TBCE_HUMAN TBCE_HUMAN]] Tubulin-folding protein; involved in the second step of the tubulin folding pathway. Seems to be implicated in the maintenance of the neuronal microtubule network. Involved in regulation of tubulin heterodimer dissociation.<ref>PMID:11847227</ref> | [[http://www.uniprot.org/uniprot/TBCE_HUMAN TBCE_HUMAN]] Tubulin-folding protein; involved in the second step of the tubulin folding pathway. Seems to be implicated in the maintenance of the neuronal microtubule network. Involved in regulation of tubulin heterodimer dissociation.<ref>PMID:11847227</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tubulin proteostasis is regulated by a group of molecular chaperones termed tubulin cofactors (TBC). Whereas tubulin heterodimer formation is well-characterized biochemically, its dissociation pathway is not clearly understood. Here, we carried out biochemical assays to dissect the role of the human TBCE and TBCB chaperones in alpha-tubulin-beta-tubulin dissociation. We used electron microscopy and image processing to determine the three-dimensional structure of the human TBCE, TBCB and alpha-tubulin (alphaEB) complex, which is formed upon alpha-tubulin-beta-tubulin heterodimer dissociation by the two chaperones. Docking the atomic structures of domains of these proteins, including the TBCE UBL domain, as we determined by X-ray crystallography, allowed description of the molecular architecture of the alphaEB complex. We found that heterodimer dissociation is an energy-independent process that takes place through a disruption of the alpha-tubulin-beta-tubulin interface that is caused by a steric interaction between beta-tubulin and the TBCE cytoskeleton-associated protein glycine-rich (CAP-Gly) and leucine-rich repeat (LRR) domains. The protruding arrangement of chaperone ubiquitin-like (UBL) domains in the alphaEB complex suggests that there is a direct interaction of this complex with the proteasome, thus mediating alpha-tubulin degradation. | ||
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| + | The structure of the complex between alpha-tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanism.,Serna M, Carranza G, Martin-Benito J, Janowski R, Canals A, Coll M, Zabala JC, Valpuesta JM J Cell Sci. 2015 May 1;128(9):1824-34. doi: 10.1242/jcs.167387. Epub 2015 Apr 23. PMID:25908846<ref>PMID:25908846</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4icv" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 15:37, 23 June 2016
Ubiquitin-like domain of human tubulin folding cofactor E - crystal form B
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