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A supramodular FHA/BRCT-repeat architecture mediates Nbs1 adaptor function in response to DNA damage.

Abstract:

The Mre11/Rad50/Nbs1 protein complex plays central enzymatic and signaling roles in the DNA-damage response. Nuclease (Mre11) and scaffolding (Rad50) components of MRN have been extensively characterized, but the molecular basis of Nbs1 function has remained elusive. Here, we present a 2.3A crystal structure of the N-terminal region of fission yeast Nbs1, revealing an unusual but conserved architecture in which the FHA- and BRCT-repeat domains structurally coalesce. We demonstrate that diphos...

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Publisher copy:
10.1016/j.cell.2009.07.043

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Journal:
Cell
Volume:
139
Issue:
1
Pages:
100-111
Publication date:
2009-10-05
DOI:
EISSN:
1097-4172
ISSN:
0092-8674
URN:
uuid:1afff16c-991c-4d39-91f0-46abd4599b19
Source identifiers:
418057
Local pid:
pubs:418057

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