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

19 Aug 2010

Abstract excerpt

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...

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PMID: 20724438
DOI: 10.1093/nar/gkq743

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Structure and function of the Rad9-binding region of the DNA-damage checkpoint adaptor TopBP1PMID 20724438Read ↗

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Phospho-epitope binding by the BRCT domains of hPTIP controls multiple aspects of the cellular response to DNA damageSemantic proximity Read ↗

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Chk1 activation requires Rad9 S/TQ-site phosphorylation to promote association with C-terminal BRCT domains of Rad4TOPBP1.Semantic proximity Read ↗

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