3SI5

Kinetochore-BUBR1 kinase complex

3SI5 の概要

• エントリーDOI: 10.2210/pdb3si5/pdb
• 関連するPDBエントリー: 2I3S 2LAH 2WVI 3E7E 3ESL
• 分子名称: Mitotic checkpoint serine/threonine-protein kinase BUB1 beta, Protein CASC5 (3 entities in total)
• 機能のキーワード: bubr1-blinkin complex, mitotic checkpoint, bubr1, blinkin/knl1, chromosome segregation, cell cycle
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: O60566; Nucleus: Q8NG31
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 46471.26

構造登録者

Blundell, T.L.,Chirgadze, D.Y.,Bolanos-Garcia, V.M. (登録日: 2011-06-17, 公開日: 2011-10-26, 最終更新日: 2023-09-13)

主引用文献

Bolanos-Garcia, V.M.,Lischetti, T.,Matak-Vinkovic, D.,Cota, E.,Simpson, P.J.,Chirgadze, D.Y.,Spring, D.R.,Robinson, C.V.,Nilsson, J.,Blundell, T.L.
Structure of a Blinkin-BUBR1 Complex Reveals an Interaction Crucial for Kinetochore-Mitotic Checkpoint Regulation via an Unanticipated Binding Site.
Structure, 19:1691-1700, 2011

PubMed Abstract: The maintenance of genomic stability relies on the spindle assembly checkpoint (SAC), which ensures accurate chromosome segregation by delaying the onset of anaphase until all chromosomes are properly bioriented and attached to the mitotic spindle. BUB1 and BUBR1 kinases are central for this process and by interacting with Blinkin, link the SAC with the kinetochore, the macromolecular assembly that connects microtubules with centromeric DNA. Here, we identify the Blinkin motif critical for interaction with BUBR1, define the stoichiometry and affinity of the interaction, and present a 2.2 Å resolution crystal structure of the complex. The structure defines an unanticipated BUBR1 region responsible for the interaction and reveals a novel Blinkin motif that undergoes a disorder-to-order transition upon ligand binding. We also show that substitution of several BUBR1 residues engaged in binding Blinkin leads to defects in the SAC, thus providing the first molecular details of the recognition mechanism underlying kinetochore-SAC signaling.

PubMed: 22000412
DOI: 10.1016/j.str.2011.09.017

実験手法

X-RAY DIFFRACTION (2.2 Å)