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Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint.

Abstract:

The spindle checkpoint protein Mad1 recruits Mad2 to unattached kinetochores and is essential for Mad2-Cdc20 complex formation in vivo but not in vitro. The crystal structure of the Mad1-Mad2 complex reveals an asymmetric tetramer, with elongated Mad1 monomers parting from a coiled-coil to form two connected sub-complexes with Mad2. The Mad2 C-terminal tails are hinged mobile elements wrapping around the elongated ligands like molecular 'safety belts'. We show that Mad1 is a competitive inhib...

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Publication status:
Published

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Publisher copy:
10.1093/emboj/21.10.2496

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Role:
Author
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Journal:
The EMBO journal
Volume:
21
Issue:
10
Pages:
2496-2506
Publication date:
2002-05-05
DOI:
EISSN:
1460-2075
ISSN:
0261-4189
URN:
uuid:72a2f431-d9fd-4e8d-b1e0-a097384faf34
Source identifiers:
375458
Local pid:
pubs:375458

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