1DUJ

SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN HUMAN MAD2

1DUJ の概要

• エントリーDOI: 10.2210/pdb1duj/pdb
• NMR情報: BMRB: 4775
• 分子名称: SPINDLE ASSEMBLY CHECKPOINT PROTEIN (1 entity in total)
• 機能のキーワード: mad2, spindle assembly checkpoint, cell cycle
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21430.37

構造登録者

Luo, X.,Fang, G.,Coldiron, M.,Lin, Y.,Yu, H. (登録日: 2000-01-17, 公開日: 2000-03-08, 最終更新日: 2024-05-22)

主引用文献

Luo, X.,Fang, G.,Coldiron, M.,Lin, Y.,Yu, H.,Kirschner, M.W.,Wagner, G.
Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20.
Nat.Struct.Biol., 7:224-229, 2000

PubMed Abstract: The checkpoint protein Mad2 inhibits the activity of the anaphase promoting complex by sequestering Cdc20 until all chromosomes are aligned at the metaphase plate. We report the solution structure of human Mad2 and its interaction with Cdc20. Mad2 possesses a novel three-layered alpha/beta fold with three alpha-helices packed between two beta-sheets. Using deletion mutants we identified the minimal Mad2-binding region of human Cdc20 as a 40-residue segment immediately N-terminal to the WD40 repeats. Mutagenesis and NMR titration experiments show that a C-terminal flexible region of Mad2 is required for binding to Cdc20. Mad2 and Cdc20 form a tight 1:1 heterodimeric complex in which the C-terminal segment of Mad2 becomes folded. These results provide the first structural insight into mechanisms of the spindle assembly checkpoint.

PubMed: 10700282
DOI: 10.1038/73338

実験手法

SOLUTION NMR