5t58
From Proteopedia
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<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=5t58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t58 OCA], [http://pdbe.org/5t58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t58 RCSB], [http://www.ebi.ac.uk/pdbsum/5t58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t58 ProSAT]</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=5t58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t58 OCA], [http://pdbe.org/5t58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t58 RCSB], [http://www.ebi.ac.uk/pdbsum/5t58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t58 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Kinetochores connect centromeric nucleosomes with mitotic-spindle microtubules through conserved, cross-interacting protein subassemblies. In budding yeast, the heterotetrameric MIND complex (Mtw1, Nnf1, Nsl1, Dsn1), ortholog of the metazoan Mis12 complex, joins the centromere-proximal components, Mif2 and COMA, with the principal microtubule-binding component, the Ndc80 complex (Ndc80C). We report the crystal structure of Kluyveromyces lactis MIND and examine its partner interactions, to understand the connection from a centromeric nucleosome to a much larger microtubule. MIND resembles an elongated, asymmetric Y; two globular heads project from a coiled-coil shaft. An N-terminal extension of Dsn1 from one head regulates interactions of the other head, blocking binding of Mif2 and COMA. Dsn1 phosphorylation by Ipl1/Aurora B relieves this autoinhibition, enabling MIND to join an assembling kinetochore. A C-terminal extension of Dsn1 recruits Ndc80C to the opposite end of the shaft. The structure and properties of MIND show how it integrates phospho-regulatory inputs for kinetochore assembly and disassembly. | ||
+ | |||
+ | Structure of the MIND Complex Defines a Regulatory Focus for Yeast Kinetochore Assembly.,Dimitrova YN, Jenni S, Valverde R, Khin Y, Harrison SC Cell. 2016 Nov 3;167(4):1014-1027.e12. doi: 10.1016/j.cell.2016.10.011. Epub 2016, Oct 27. PMID:27881300<ref>PMID:27881300</ref> | ||
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+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 5t58" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 14:20, 22 December 2016
Structure of the MIND Complex Shows a Regulatory Focus of Yeast Kinetochore Assembly
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Categories: Dimitrova, Y | Harrison, S C | Jenni, S | Khin, Y | Valverde, R | Cell cycle | Chromosome | Complex | Kinetochore | Mind | Mis12 | Mtw1 complex | Segregation