1duj
SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN HUMAN MAD2
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OverviewOverview
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.
About this StructureAbout this Structure
1DUJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20., Luo X, Fang G, Coldiron M, Lin Y, Yu H, Kirschner MW, Wagner G, Nat Struct Biol. 2000 Mar;7(3):224-9. PMID:10700282
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