3VZA

Crystal structure of the chicken Spc24-Spc25 globular domain in complex with CENP-T peptide

3VZA の概要

• エントリーDOI: 10.2210/pdb3vza/pdb
• 関連するPDBエントリー: 3VZ9
• 分子名称: Uncharacterized protein, Spc24 protein, Centromere protein T, ... (4 entities in total)
• 機能のキーワード: rwd domain, kinetochore component, chromosome segregation, ndc80 complex, cell cycle
• 由来する生物種: Gallus gallus (chicken); 詳細
• 細胞内の位置: Nucleus: F1NPG5
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 50684.97

構造登録者

Nishino, T.,Fukagawa, T. (登録日: 2012-10-09, 公開日: 2013-04-03, 最終更新日: 2023-11-08)

主引用文献

Nishino, T.,Rago, F.,Hori, T.,Tomii, K.,Cheeseman, I.M.,Fukagawa, T.
CENP-T provides a structural platform for outer kinetochore assembly
Embo J., 32:424-436, 2013

PubMed Abstract: The kinetochore forms a dynamic interface with microtubules from the mitotic spindle during mitosis. The Ndc80 complex acts as the key microtubule-binding complex at kinetochores. However, it is unclear how the Ndc80 complex associates with the inner kinetochore proteins that assemble upon centromeric chromatin. Here, based on a high-resolution structural analysis, we demonstrate that the N-terminal region of vertebrate CENP-T interacts with the 'RWD' domain in the Spc24/25 portion of the Ndc80 complex. Phosphorylation of CENP-T strengthens a cryptic hydrophobic interaction between CENP-T and Spc25 resulting in a phospho-regulated interaction that occurs without direct recognition of the phosphorylated residue. The Ndc80 complex interacts with both CENP-T and the Mis12 complex, but we find that these interactions are mutually exclusive, supporting a model in which two distinct pathways target the Ndc80 complex to kinetochores. Our results provide a model for how the multiple protein complexes at kinetochores associate in a phospho-regulated manner.

PubMed: 23334297
DOI: 10.1038/emboj.2012.348

実験手法

X-RAY DIFFRACTION (1.898 Å)