5gpl

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'''Unreleased structure'''
 
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The entry 5gpl is ON HOLD until Paper Publication
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==Crystal structure of Ccp1==
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<StructureSection load='5gpl' size='340' side='right' caption='[[5gpl]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5gpl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GPL FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gpk|5gpk]]</td></tr>
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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=5gpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gpl OCA], [http://pdbe.org/5gpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gpl RCSB], [http://www.ebi.ac.uk/pdbsum/5gpl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gpl ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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CENP-A is a centromere-specific histone 3 variant essential for centromere specification. CENP-A partially replaces canonical histone H3 at the centromeres. How the particular CENP-A/H3 ratio at centromeres is precisely maintained is unknown. It also remains unclear how CENP-A is excluded from non-centromeric chromatin. Here, we identify Ccp1, an uncharacterized NAP family protein in fission yeast that antagonizes CENP-A loading at both centromeric and non-centromeric regions. Like the CENP-A loading factor HJURP, Ccp1 interacts with CENP-A and is recruited to centromeres at the end of mitosis in a Mis16-dependent manner. These data indicate that factors with opposing CENP-A loading activities are recruited to centromeres. Furthermore, Ccp1 also cooperates with H2A.Z to evict CENP-A assembled in euchromatin. Structural analyses indicate that Ccp1 forms a homodimer that is required for its anti-CENP-A loading activity. Our study establishes mechanisms for maintenance of CENP-A homeostasis at centromeres and the prevention of ectopic assembly of centromeres.
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Authors: Yin, F., Gao, F., Chen, Y.
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Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading.,Dong Q, Yin FX, Gao F, Shen Y, Zhang F, Li Y, He H, Gonzalez M, Yang J, Zhang S, Su M, Chen YH, Li F Mol Cell. 2016 Oct 6;64(1):79-91. doi: 10.1016/j.molcel.2016.08.022. Epub 2016, Sep 22. PMID:27666591<ref>PMID:27666591</ref>
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Description: Crystal structure of Ccp1
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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 5gpl" 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: Chen, Y]]
[[Category: Chen, Y]]
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[[Category: Yin, F]]
 
[[Category: Gao, F]]
[[Category: Gao, F]]
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[[Category: Yin, F]]
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[[Category: Ccp1 dimer]]
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[[Category: Chaperone]]
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[[Category: Nucleosome assembly protein]]

Revision as of 18:33, 10 December 2016

Crystal structure of Ccp1

5gpl, resolution 2.10Å

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