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2KDD

Solution structure of the conserved C-terminal dimerization domain of Borealin

2KDD の概要
エントリーDOI10.2210/pdb2kdd/pdb
NMR情報BMRB: 16110
分子名称Borealin (1 entity in total)
機能のキーワードprotein dimer, cell cycle, cell division, centromere, chromosomal protein, cytoplasm, mitosis, nucleus, phosphoprotein, polymorphism
由来する生物種Homo sapiens (human)
タンパク質・核酸の鎖数2
化学式量合計16164.31
構造登録者
Lingel, A.,Bourhis, E.,Cochran, A.G.,Fairbrother, W.J. (登録日: 2009-01-06, 公開日: 2009-06-30, 最終更新日: 2024-05-08)
主引用文献Bourhis, E.,Lingel, A.,Phung, Q.,Fairbrother, W.J.,Cochran, A.G.
Phosphorylation of a borealin dimerization domain is required for proper chromosome segregation.
Biochemistry, 48:6783-6793, 2009
Cited by
PubMed Abstract: The chromosomal passenger complex (CPC) has been identified as a master regulator of mitosis. In particular, proper chromosome segregation and cytokinesis depend on the correct localization and function of the CPC. Within the complex, the kinase Aurora B associates with Incenp, Survivin, and Borealin. The stoichiometry of the complex as well as a complete understanding of how these four components interact with each other remains to be elucidated. Here, we identify a new domain of Borealin. We determined its structure using NMR spectroscopy and discovered a novel dimerization motif. Interestingly, we found that substitutions at Borealin T230, recently identified as an Mps1 phosphorylation site, can modulate the dimerization state of Borealin. Mutation of this single residue to alanine or valine impairs Aurora B activity during mitosis and causes chromosome segregation defects. This study reveals that Mps1 regulates the CPC through a novel Borealin domain.
PubMed: 19530738
DOI: 10.1021/bi900530v
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2kdd
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-12-18に公開中

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