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1duj
From Proteopedia
| 1duj, 1 NMR models () | |||||||||
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| Domains: | HORMA | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN HUMAN MAD2
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1DUJ is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- Luo X, Fang G, Coldiron M, Lin Y, Yu H, Kirschner MW, Wagner G. Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20. Nat Struct Biol. 2000 Mar;7(3):224-9. PMID:10700282 doi:10.1038/73338
Page seeded by OCA on Tue Feb 17 13:00:30 2009
