5LSJ

CRYSTAL STRUCTURE OF THE HUMAN KINETOCHORE MIS12-CENP-C delta-HEAD2 COMPLEX

5LSJ の概要

• エントリーDOI: 10.2210/pdb5lsj/pdb
• 分子名称: Protein MIS12 homolog, Polyamine-modulated factor 1, Kinetochore-associated protein DSN1 homolog, ... (5 entities in total)
• 機能のキーワード: alpha-helical, cell cycle
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Chromosome, centromere, kinetochore : Q9H081; Nucleus : Q6P1K2 Q9H410 Q96IY1 Q03188
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 173558.23

構造登録者

Vetter, I.R.,Petrovic, A.,Keller, J.,Liu, Y. (登録日: 2016-09-02, 公開日: 2016-11-16, 最終更新日: 2024-01-17)

主引用文献

Petrovic, A.,Keller, J.,Liu, Y.,Overlack, K.,John, J.,Dimitrova, Y.N.,Jenni, S.,van Gerwen, S.,Stege, P.,Wohlgemuth, S.,Rombaut, P.,Herzog, F.,Harrison, S.C.,Vetter, I.R.,Musacchio, A.
Structure of the MIS12 Complex and Molecular Basis of Its Interaction with CENP-C at Human Kinetochores.
Cell, 167:1028-1040.e15, 2016

PubMed Abstract: Kinetochores, multisubunit protein assemblies, connect chromosomes to spindle microtubules to promote chromosome segregation. The 10-subunit KMN assembly (comprising KNL1, MIS12, and NDC80 complexes, designated KNL1C, MIS12C, and NDC80C) binds microtubules and regulates mitotic checkpoint function through NDC80C and KNL1C, respectively. MIS12C, on the other hand, connects the KMN to the chromosome-proximal domain of the kinetochore through a direct interaction with CENP-C. The structural basis for this crucial bridging function of MIS12C is unknown. Here, we report crystal structures of human MIS12C associated with a fragment of CENP-C and unveil the role of Aurora B kinase in the regulation of this interaction. The structure of MIS12:CENP-C complements previously determined high-resolution structures of functional regions of NDC80C and KNL1C and allows us to build a near-complete structural model of the KMN assembly. Our work illuminates the structural organization of essential chromosome segregation machinery that is conserved in most eukaryotes.

PubMed: 27881301
DOI: 10.1016/j.cell.2016.10.005

実験手法

X-RAY DIFFRACTION (3.25 Å)