Nucl._Acids_Res.-2011-Rappas-313-24.pdf (4.96 MB)
Structure and function of the Rad9-binding region of the DNA-damage checkpoint adaptor TopBP1
journal contribution
posted on 2023-06-07, 20:21 authored by Mathieu Rappas, Antony OliverAntony Oliver, Laurence PearlLaurence PearlTopBP1 is a scaffold protein that coordinates activation of the DNA-damage-checkpoint response by coupling binding of the 9-1-1 checkpoint clamp at sites of ssDNA, to activation of the ATR-ATRIP checkpoint kinase complex. We have now determined the crystal structure of the N-terminal region of human TopBP1, revealing an unexpected triple-BRCT domain structure. The arrangement of the BRCT domains differs significantly from previously described tandem BRCT domain structures, and presents two distinct sites for binding phosphopeptides in the second and third BRCT domains. We show that the site in the second but not third BRCT domain in the N-terminus of TopBP1, provides specific interaction with a phosphorylated motif at pSer387 in Rad9, which can be generated by CK2.
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Publication status
- Published
File Version
- Published version
Journal
Nucleic Acids ResearchISSN
0305-1048External DOI
Issue
1Volume
39Page range
313-324Department affiliated with
- Sussex Centre for Genome Damage Stability Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06First Open Access (FOA) Date
2016-03-22First Compliant Deposit (FCD) Date
2016-11-18Usage metrics
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