The structural basis for partitioning of the XRCC1/DNA ligase III-&#945; BRCT-mediated dimer complexes.

Cuneo, Matthew J; Gabel, Scott A; Krahn, Joseph M; Ricker, Melissa A; London, Robert E

The structural basis for partitioning of the XRCC1/DNA ligase III-α BRCT-mediated dimer complexes.

Cuneo, Matthew J; Gabel, Scott A; Krahn, Joseph M; Ricker, Melissa A; London, Robert E.

Affiliation

Cuneo MJ; National Institute of Environmental Health Sciences, NIH, DHHS, Research Triangle Park, NC, USA.

Nucleic Acids Res ; 39(17): 7816-27, 2011 Sep 01.

Article in En | MEDLINE | ID: mdl-21652643

Subject(s)

DNA Ligases/chemistry; DNA-Binding Proteins/chemistry; Amino Acid Sequence; Animals; Chromatography, Gel; Crystallography, X-Ray; DNA Ligase ATP; DNA-Binding Proteins/genetics; Dimerization; Humans; Mice; Models, Molecular; Molecular Sequence Data; Mutation; Poly-ADP-Ribose Binding Proteins; Protein Structure, Tertiary; Scattering, Small Angle; X-Ray Diffraction; X-ray Repair Cross Complementing Protein 1; Xenopus Proteins

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: DNA Ligases / DNA-Binding Proteins Limits: Animals / Humans Language: En Journal: Nucleic Acids Res Year: 2011 Document type: Article Affiliation country: United States Country of publication: United kingdom

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