Solution structure of polymerase μ's BRCT domain reveals an element essential for its role in nonhomologous end joining

Biochemistry

Volumn 46, Issue 43, 2007, Pages 12100-12110

  DeRose, Eugene F ^a   Clarkson, Michael W ^b   Gilmore, Steven A ^c   Galban, Cristina J ^c   Tripathy, Ashutosh ^b   Havener, Jody M ^b,c   Mueller, Geoffrey A ^a   Ramsden, Dale A ^b,c   London, Robert E ^a   Lee, Andrew L ^b,c  

^a NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES   (United States)

^b UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA DAMAGE; HOMODIMERS; HUMAN DNA POLYMERASE; MUTATION;

CHROMOSOMES; DIMERS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; SOLVENTS;

DNA;

AMINO ACID; ARGININE; DNA POLYMERASE; DNA POLYMERASE MU; KU ANTIGEN; LIGASE; PROLINE; UNCLASSIFIED DRUG; XRCC4 LIGASE IV;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; CHROMOSOME BREAKAGE; DNA REPAIR; DYNAMICS; ENZYME ACTIVITY; HUMAN; HYDROPHOBICITY; NONHOMOLOGOUS END JOINING; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; DNA PRIMERS; DNA-DIRECTED DNA POLYMERASE; ELECTROPHORETIC MOBILITY SHIFT ASSAY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 35648951054     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7007728     Document Type: Article

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