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Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the gamma-H2AX histone tail

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dc.contributor.author Lee, M. S. en_US
dc.contributor.author Edwards, R. A. en_US
dc.contributor.author Thede, G. L. en_US
dc.contributor.author Glover, J. N. en_US
dc.date.accessioned 2006-06-22T14:16:35Z
dc.date.available 2006-06-22T14:16:35Z
dc.date.issued 2005-09 en_US
dc.identifier.citation J Biol Chem 280, 32053-6 (2005) en_US
dc.identifier.uri http://hdl.handle.net/1807.1/161
dc.description This article is hosted on a website external to the CBCRA Open Access Archive. Selecting “View/Open” below will launch the full-text article in another browser window.
dc.description.abstract MDC1 (mediator of DNA damage checkpoint protein 1) regulates the recognition and repair of DNA double strand breaks in mammalian cells through its interactions with nuclear foci containing the COOH-terminally phosphorylated form of the histone variant, H2AX. Here we demonstrate that the tandem BRCT repeats of MDC1 directly bind to the phosphorylated tail of H2AX-Ser(P)-Gln-Glu-Tyr, in a manner that is critically dependent on the free carboxylate group of the COOH-terminal Tyr residue. We have determined the x-ray crystal structure of the MDC1 BRCT repeats at 1.45 Angstroms resolution. By a comparison with the structure of the BRCA1 BRCT bound to a phosphopeptide, we suggest that two arginine residues in MDC1, Arg(1932) and Arg(1933) may recognize the COOH terminus of the peptide as well as the penultimate Glu of H2AX, while Gln(2013) may provide additional specificity for the COOH-terminal Tyr. en_US
dc.description.provenance Made available in DSpace on 2006-06-22T14:16:35Z (GMT). No. of bitstreams: 1 Lee.2005.32053.html: 415 bytes, checksum: 865e7b862e6facf7a56fcde1eed9cc39 (MD5) Previous issue date: 2005-09 en
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dc.language.iso en en_US
dc.publisher American Society for Biochemistry and Molecular Biology en_US
dc.relation.uri http://www.asbmb.org/ en_US
dc.title Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the gamma-H2AX histone tail en_US
dc.type Article en_US

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