The formation of a salt bridge between helices 3 and 6 is responsible for the constitutive activity and lack of hormone responsiveness of the naturally occurring L457R mutation of the human lutropin receptor

Journal of Biological Chemistry

Volumn 280, Issue 28, 2005, Pages 26169-26176

  Zhang, Meilin ^a   Mizrachi, Dario ^a   Fanelli, Francesca ^b   Segaloff, Deborah L ^a  

^a UNIVERSITY OF IOWA   (United States)

^b UNIVERSITY OF MODENA AND REGGIO EMILIA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CYTOLOGY; ENDOCRINOLOGY; MUTAGENESIS; STRUCTURAL ANALYSIS;

HUMAN LUTROPIN RECEPTOR (HLHR); MUTATIONS; VITRO EXPERIMENTS;

HORMONES;

ARGININE; ASPARAGINE; ASPARTIC ACID; BRIDGED PEPTIDE; G PROTEIN COUPLED RECEPTOR; LEUCINE; LUTEINIZING HORMONE RECEPTOR; MUTANT PROTEIN; RHODOPSIN; RHODOPSIN LIKE G PROTEIN COUPLED RECEPTOR; SOLVENT; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; ENDOCRINOLOGY; GENE DISRUPTION; HORMONE RESPONSE; HUMAN; HUMAN CELL; MOLECULAR INTERACTION; MUTATION; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN STABILITY; PROTEIN STRUCTURE; RECEPTOR UPREGULATION; RECIPROCAL CHROMOSOME TRANSLOCATION; REPRODUCTION; SALT BRIDGE;

AMINO ACID MOTIFS; ARGININE; ASPARAGINE; BINDING SITES; CELL LINE; CELL MEMBRANE; CHORIONIC GONADOTROPIN; CRYSTALLOGRAPHY, X-RAY; CYCLIC AMP; CYTOSOL; DNA, COMPLEMENTARY; HETEROZYGOTE; HUMANS; HYDROGEN BONDING; LEUCINE; MODELS, MOLECULAR; MUTAGENESIS; MUTATION; PHENOTYPE; PLASMIDS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, G-PROTEIN-COUPLED; RECEPTORS, LH; RHODOPSIN; SALTS; SOFTWARE;

EID: 22544468863     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M502102200     Document Type: Article

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