1DUJ

SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN HUMAN MAD2

Summary for 1DUJ

• Entry DOI: 10.2210/pdb1duj/pdb
• NMR Information: BMRB: 4775
• Descriptor: SPINDLE ASSEMBLY CHECKPOINT PROTEIN (1 entity in total)
• Functional Keywords: mad2, spindle assembly checkpoint, cell cycle
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 21430.37

Authors

Luo, X.,Fang, G.,Coldiron, M.,Lin, Y.,Yu, H. (deposition date: 2000-01-17, release date: 2000-03-08, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

SOLUTION NMR