View source for 5gpl


==Crystal structure of Ccp1==
<StructureSection load='5gpl' size='340' side='right'caption='[[5gpl]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gpl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5GPL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gpl OCA], [https://pdbe.org/5gpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gpl RCSB], [https://www.ebi.ac.uk/pdbsum/5gpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gpl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YO48_SCHPO YO48_SCHPO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5gpl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe 972h-]]
[[Category: Chen Y]]
[[Category: Gao F]]
[[Category: Yin F]]