5lsj

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m (Protected "5lsj" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5lsj is ON HOLD
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==CRYSTAL STRUCTURE OF THE HUMAN KINETOCHORE MIS12-CENP-C delta-HEAD2 COMPLEX==
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<StructureSection load='5lsj' size='340' side='right' caption='[[5lsj]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5lsj]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LSJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LSJ FirstGlance]. <br>
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</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=5lsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lsj OCA], [http://pdbe.org/5lsj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lsj RCSB], [http://www.ebi.ac.uk/pdbsum/5lsj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lsj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/NSL1_HUMAN NSL1_HUMAN]] Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis.<ref>PMID:16585270</ref> [[http://www.uniprot.org/uniprot/MIS12_HUMAN MIS12_HUMAN]] Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis (PubMed:12515822, PubMed:15502821, PubMed:16585270). Essential for proper kinetochore microtubule attachments (PubMed:23891108).<ref>PMID:12515822</ref> <ref>PMID:15502821</ref> <ref>PMID:16585270</ref> <ref>PMID:23891108</ref> [[http://www.uniprot.org/uniprot/DSN1_HUMAN DSN1_HUMAN]] Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis.<ref>PMID:15502821</ref> <ref>PMID:16585270</ref> [[http://www.uniprot.org/uniprot/PMF1_HUMAN PMF1_HUMAN]] Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT.<ref>PMID:10419538</ref> <ref>PMID:11256947</ref> <ref>PMID:15502821</ref> <ref>PMID:16585270</ref> [[http://www.uniprot.org/uniprot/CENPC_HUMAN CENPC_HUMAN]] Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions.<ref>PMID:19482874</ref> <ref>PMID:21529714</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Kinetochores, multisubunit protein assemblies, connect chromosomes to spindle microtubules to promote chromosome segregation. The 10-subunit KMN assembly (comprising KNL1, MIS12, and NDC80 complexes, designated KNL1C, MIS12C, and NDC80C) binds microtubules and regulates mitotic checkpoint function through NDC80C and KNL1C, respectively. MIS12C, on the other hand, connects the KMN to the chromosome-proximal domain of the kinetochore through a direct interaction with CENP-C. The structural basis for this crucial bridging function of MIS12C is unknown. Here, we report crystal structures of human MIS12C associated with a fragment of CENP-C and unveil the role of Aurora B kinase in the regulation of this interaction. The structure of MIS12:CENP-C complements previously determined high-resolution structures of functional regions of NDC80C and KNL1C and allows us to build a near-complete structural model of the KMN assembly. Our work illuminates the structural organization of essential chromosome segregation machinery that is conserved in most eukaryotes.
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Authors: Vetter, I.R., Petrovic, A., Keller, J., Liu, Y.
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Structure of the MIS12 Complex and Molecular Basis of Its Interaction with CENP-C at Human Kinetochores.,Petrovic A, Keller J, Liu Y, Overlack K, John J, Dimitrova YN, Jenni S, van Gerwen S, Stege P, Wohlgemuth S, Rombaut P, Herzog F, Harrison SC, Vetter IR, Musacchio A Cell. 2016 Nov 3;167(4):1028-1040.e15. doi: 10.1016/j.cell.2016.10.005. Epub 2016, Oct 27. PMID:27881301<ref>PMID:27881301</ref>
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Description: CRYSTAL STRUCTURE OF THE HUMAN KINETOCHORE MIS12-CENP-C delta-HEAD2 COMPLEX
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5lsj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Keller, J]]
[[Category: Keller, J]]
[[Category: Liu, Y]]
[[Category: Liu, Y]]
[[Category: Petrovic, A]]
[[Category: Petrovic, A]]
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[[Category: Vetter, I.R]]
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[[Category: Vetter, I R]]
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[[Category: Alpha-helical]]
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[[Category: Cell cycle]]

Revision as of 19:41, 9 December 2016

CRYSTAL STRUCTURE OF THE HUMAN KINETOCHORE MIS12-CENP-C delta-HEAD2 COMPLEX

5lsj, resolution 3.25Å

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