Mutation of a single TMVI residue, Phe282, in the β2-adrenergic receptor results in structurally distinct activated receptor conformations

Biochemistry

Volumn 41, Issue 19, 2002, Pages 6045-6053

  Chen, Songhai ^a,b   Lin, F Fang ^a,b   Xu, Ming ^a   Riek, R Peter ^a   Novotny, Jiri ^a   Graham, Robert M ^a,c  

^a ST VINCENT S HOSPITAL   (Australia)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF NEW SOUTH WALES   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

AGONIST BINDING;

PROTEINS;

BIOCHEMISTRY;

ALANINE; ASPARAGINE; BETA 2 ADRENERGIC RECEPTOR; CYSTEINE; G PROTEIN COUPLED RECEPTOR; GLYCINE; ISOPRENALINE; LEUCINE; PHENYLALANINE; PROLINE;

ANIMAL CELL; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; GENE MUTATION; GENETIC TRANSFECTION; LIGAND BINDING; MOLECULAR MODEL; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN TRANSPORT; RECEPTOR DENSITY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; COMPUTER SIMULATION; CONSERVED SEQUENCE; COS CELLS; CRICETINAE; GTP-BINDING PROTEINS; KINETICS; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, ADRENERGIC, BETA-2; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

ANIMALIA;

EID: 0037076531     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi012189c     Document Type: Article

References (35)