Arg278, but not Lys229 or Lys236, plays an important role in the binding of retinoic acid by retinoic acid receptor γ

Journal of Biological Chemistry

Volumn 273, Issue 51, 1998, Pages 34016-34021

  Zhang, Zhen Ping ^a   Gambone, Carlo J ^a   Gabriel, Jerome L ^a   Wolfgang, Christopher L ^a   Soprano, Kenneth J ^a   Soprano, Dianne Robert ^a  

^a TEMPLE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

RETINOIC ACID; RETINOID X RECEPTOR; ARGININE; LYSINE; PRIMER DNA; RECOMBINANT PROTEIN; RETINOIC ACID RECEPTOR; RETINOIC ACID RECEPTOR GAMMA;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; HORMONE RECEPTOR INTERACTION; PRIORITY JOURNAL; PROTEIN FOLDING; RECEPTOR AFFINITY; SEQUENCE HOMOLOGY; AMINO ACID SUBSTITUTION; ANIMAL; CHEMISTRY; KINETICS; METABOLISM; MOUSE; POLYMERASE CHAIN REACTION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; ANIMALS; ARGININE; BINDING SITES; DNA PRIMERS; KINETICS; LYSINE; MICE; MUTAGENESIS, SITE-DIRECTED; POLYMERASE CHAIN REACTION; PROTEIN FOLDING; RECEPTORS, RETINOIC ACID; RECOMBINANT PROTEINS; TRETINOIN;

EID: 0032545102     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.51.34016     Document Type: Article

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