View source for 7kys


==Crystal structure of human BCCIP beta (Native2)==
<StructureSection load='7kys' size='340' side='right'caption='[[7kys]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7kys]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KYS 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=7kys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kys OCA], [https://pdbe.org/7kys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kys RCSB], [https://www.ebi.ac.uk/pdbsum/7kys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kys ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BCCIP_HUMAN BCCIP_HUMAN] During interphase, required for microtubule organizing and anchoring activities. During mitosis, required for the organization and stabilization of the spindle pole (PubMed:28394342). Isoform 2/alpha is particularly important for the regulation of microtubule anchoring, microtubule stability, spindle architecture and spindle orientation, compared to isoform 1/beta (PubMed:28394342). May promote cell cycle arrest by enhancing the inhibition of CDK2 activity by CDKN1A. May be required for repair of DNA damage by homologous recombination in conjunction with BRCA2. May not be involved in non-homologous end joining (NHEJ).<ref>PMID:10878006</ref> <ref>PMID:14726710</ref> <ref>PMID:15539944</ref> <ref>PMID:15713648</ref> <ref>PMID:17947333</ref> <ref>PMID:28394342</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BCCIP was isolated based on its interactions with tumor suppressors BRCA2 and p21. Knockdown or knockout of BCCIP causes embryonic lethality in mice. BCCIP deficient cells exhibit impaired cell proliferation and chromosome instability. BCCIP also plays a key role in biogenesis of ribosome 60S subunits. BCCIP is conserved from yeast to humans, but it has no discernible sequence similarity to proteins of known structures. Here we report two crystal structures of an N-terminal truncated human BCCIPbeta, consisting of residues 61-314. Structurally BCCIP is similar to GCN5-related acetyltransferases (GNATs) but contains different sequence motifs. Moreover, both acetyl-CoA and substrate-binding grooves are altered in BCCIP. A large 19-residue flap over the putative CoA binding site adopts either an open or closed conformation in BCCIP. The substrate binding groove is significantly reduced in size and is positively charged despite the acidic isoelectric point of BCCIP. BCCIP has potential binding sites for partner proteins and may have enzymatic activity.

Structure of human BCCIP and implications for binding and modification of partner proteins.,Choi WS, Liu B, Shen Z, Yang W Protein Sci. 2021 Mar;30(3):693-699. doi: 10.1002/pro.4026. Epub 2021 Jan 29. PMID:33452718<ref>PMID:33452718</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7kys" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Choi WS]]
[[Category: Liu B]]
[[Category: Shen Z]]
[[Category: Yang W]]