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Nucleic Acids Res. 2011 Jan;39(1):313-24. doi: 10.1093/nar/gkq743. Epub 2010 Aug 19.

Structure and function of the Rad9-binding region of the DNA-damage checkpoint adaptor TopBP1.

Author information

1
Cancer Research UK DNA Repair Enzyme Group, Section of Structural Biology, The Institute of Cancer Research, London, UK.

Erratum in

  • Nucleic Acids Res. 2013 Apr;41(8):4741.

Abstract

TopBP1 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.

PMID:
20724438
PMCID:
PMC3017600
DOI:
10.1093/nar/gkq743
[Indexed for MEDLINE]
Free PMC Article

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