Mapping and quantitation of the interaction between the recombination activating gene proteins RAG1 and RAG2

Journal of Biological Chemistry

Volumn 290, Issue 19, 2015, Pages 11802-11817

  Zhang, Yu Hang ^a   Shetty, Keerthi ^a   Surleac, Marius D ^b   Petrescu, Andrei J ^b   Schatz, David G ^a,c  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b INSTITUTE OF BIOCHEMISTRY OF THE ROMANIAN ACADEMY   (Romania)

^c HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CATALYSIS; CHEMICAL ACTIVATION; GENES;

ACIDIC AMINO ACIDS; BINDING AFFINITIES; CATALYTIC CENTER; CATALYTIC FUNCTIONS; RECOMBINATION ACTIVATING GENES; RECOMBINATION ACTIVITY; STRUCTURAL MODELING; WESTERN BLOTTING;

AMINO ACIDS;

ASPARTIC ACID; GLUTAMIC ACID; LYSINE; RAG1 PROTEIN; RAG2 PROTEIN; UNCLASSIFIED DRUG; ZINC FINGER B PROTEIN; ZINC FINGER PROTEIN; DNA BINDING PROTEIN; HOMEODOMAIN PROTEIN; NUCLEAR PROTEIN; PROTEIN BINDING; RAG-1 PROTEIN; RAG2 PROTEIN, HUMAN; RECOMBINASE;

ALPHA HELIX; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; INTERFEROMETRY; MALE; MOLECULAR MODEL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PULLDOWN ASSAY; STRUCTURE ANALYSIS; WESTERN BLOTTING; AMINO ACID SEQUENCE; ANIMAL; C57BL MOUSE; CYTOLOGY; ENZYME ACTIVE SITE; GENE EXPRESSION REGULATION; HEK293 CELL LINE; HUMAN; HUMAN GENOME; METABOLISM; MOLECULAR GENETICS; MUTATION; PROTEIN SECONDARY STRUCTURE; THYMUS; VDJ RECOMBINATION;

AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; DNA-BINDING PROTEINS; GENE EXPRESSION REGULATION; GENOME, HUMAN; HEK293 CELLS; HOMEODOMAIN PROTEINS; HUMANS; INTERFEROMETRY; MALE; MICE; MICE, INBRED C57BL; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEAR PROTEINS; PROTEIN BINDING; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, SECONDARY; THYMUS GLAND; V(D)J RECOMBINATION; VDJ RECOMBINASES;

EID: 84929191795     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.638627     Document Type: Article

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