1duj: Difference between revisions
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'''SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN HUMAN MAD2''' | '''SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN HUMAN MAD2''' | ||
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[[Category: Luo, X.]] | [[Category: Luo, X.]] | ||
[[Category: Yu, H.]] | [[Category: Yu, H.]] | ||
[[Category: | [[Category: Mad2]] | ||
[[Category: | [[Category: Spindle assembly checkpoint]] | ||
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Revision as of 14:17, 2 May 2008
SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN HUMAN MAD2
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 Page seeded by OCA on Fri May 2 14:17:33 2008