- 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...
Expand abstract - 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
- Language:
- English
- Keywords:
- Copyright date:
- 2009
Journal article
A supramodular FHA/BRCT-repeat architecture mediates Nbs1 adaptor function in response to DNA damage.
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