4x23
From Proteopedia
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| - | ''' | + | ==CRYSTAL STRUCTURE OF CENP-C IN COMPLEX WITH THE NUCLEOSOME CORE PARTICLE== |
| + | <StructureSection load='4x23' size='340' side='right' caption='[[4x23]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4x23]] is a 24 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4inm 4inm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X23 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X23 FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4inm|4inm]]</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=4x23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x23 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x23 RCSB], [http://www.ebi.ac.uk/pdbsum/4x23 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Chromosome segregation during mitosis requires assembly of the kinetochore complex at the centromere. Kinetochore assembly depends on specific recognition of the histone variant CENP-A in the centromeric nucleosome by centromere protein C (CENP-C). We have defined the determinants of this recognition mechanism and discovered that CENP-C binds a hydrophobic region in the CENP-A tail and docks onto the acidic patch of histone H2A and H2B. We further found that the more broadly conserved CENP-C motif uses the same mechanism for CENP-A nucleosome recognition. Our findings reveal a conserved mechanism for protein recruitment to centromeres and a histone recognition mode whereby a disordered peptide binds the histone tail through hydrophobic interactions facilitated by nucleosome docking. | ||
| - | + | A conserved mechanism for centromeric nucleosome recognition by centromere protein CENP-C.,Kato H, Jiang J, Zhou BR, Rozendaal M, Feng H, Ghirlando R, Xiao TS, Straight AF, Bai Y Science. 2013 May 31;340(6136):1110-3. doi: 10.1126/science.1235532. PMID:23723239<ref>PMID:23723239</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Jiang, J S]] | ||
| + | [[Category: Cenp-c complex]] | ||
| + | [[Category: Chromosome centromere]] | ||
| + | [[Category: Histone fold]] | ||
| + | [[Category: Kinetochore assembly]] | ||
| + | [[Category: Nucleosome core particle]] | ||
| + | [[Category: Segregation]] | ||
| + | [[Category: Structural protein-dna complex]] | ||
| + | [[Category: Widom 601 dna fragmment]] | ||
Revision as of 15:59, 10 December 2014
CRYSTAL STRUCTURE OF CENP-C IN COMPLEX WITH THE NUCLEOSOME CORE PARTICLE
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