DNA-binding domain within the Brh2 N terminus is the primary interaction site for association with DNA

Journal of Biological Chemistry

Volumn 284, Issue 13, 2009, Pages 8265-8273

  Zhou, Qingwen ^a   Kojic, Milorad ^a   Holloman, William K ^a  

^a WEILL CORNELL MEDICAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINAL REGIONS; DELETION MAPPING; DNA BINDING ACTIVITY; DNA REPAIR; DNA-BINDING DOMAIN; FULL-LENGTH PROTEINS; FUNCTIONAL DOMAINS; INTERACTION SITE; N-TERMINAL; REPLICATION PROTEIN A;

ASSOCIATION REACTIONS; DIELECTRIC DEVICES; DNA; GENES; MAMMALS; NUCLEIC ACIDS;

BINDING SITES;

BRCA2 PROTEIN; FUNGAL DNA; RAD51 PROTEIN; REPLICATION FACTOR A;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DNA BINDING MOTIF; DNA REPAIR; GENE DELETION; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; USTILAGO MAYDIS;

BRCA2 PROTEIN; DNA REPAIR; DNA, FUNGAL; DNA-BINDING PROTEINS; FUNGAL PROTEINS; MODELS, BIOLOGICAL; PEPTIDE MAPPING; PROTEIN STRUCTURE, TERTIARY; RAD51 RECOMBINASE; SEQUENCE HOMOLOGY, AMINO ACID; USTILAGO;

MAMMALIA; USTILAGO MAYDIS;

EID: 67649821713     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M809226200     Document Type: Article

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