Activation of the β2-Adrenergic Receptor Involves Disruption of an Ionic Lock between the Cytoplasmic Ends of Transmembrane Segments 3 and 6

Journal of Biological Chemistry

Volumn 276, Issue 31, 2001, Pages 29171-29177

  Ballesteros, Juan A ^a   Jensen, Anne D ^b,e   Liapakis, George ^c,d   Rasmussen, Søren G F ^b   Shi, Lei ^c   Gether, Ulrik ^b   Javitch, Jonathan A ^c  

^a Novasite Pharmaceuticals Inc   (United States)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

^c The New York Presbyterian Hospital   (United States)

^d UNIVERSITY OF CRETE   (Greece)

^e Maxygen APS   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CELLS; CHEMICAL ACTIVATION; CONFORMATIONS; CYTOLOGY; MUTAGENESIS; PROTEINS;

IONIC INTERACTIONS;

CELL MEMBRANES;

ARGININE; ASPARTIC ACID; BETA 2 ADRENERGIC RECEPTOR; CYCLIC AMP; CYSTEINE; G PROTEIN COUPLED RECEPTOR; GLUTAMIC ACID; MEMBRANE PROTEIN; PINDOLOL; RHODOPSIN; TRANSMEMBRANE SEGMENT 3; TRANSMEMBRANE SEGMENT 6; UNCLASSIFIED DRUG; 4 (3 TERT BUTYLAMINO 2 HYDROXYPROPOXY) 2 BENZIMIDAZOLONE; BETA ADRENERGIC RECEPTOR STIMULATING AGENT; PROPANOLAMINE DERIVATIVE; RECOMBINANT PROTEIN;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL MEMBRANE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CYTOPLASM; NONHUMAN; PRIORITY JOURNAL; RECEPTOR BINDING; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL; CELL LINE; CELL STRAIN COS1; CERCOPITHECUS; CHEMICAL STRUCTURE; CHEMISTRY; GENETIC TRANSFECTION; HUMAN; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PHYSIOLOGY; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

ANIMALIA;

ADRENERGIC BETA-AGONISTS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; ARGININE; ASPARTIC ACID; CELL LINE; CELL MEMBRANE; CERCOPITHECUS AETHIOPS; CONSERVED SEQUENCE; COS CELLS; CYCLIC AMP; CYTOPLASM; GLUTAMIC ACID; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROPANOLAMINES; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, ADRENERGIC, BETA-2; RECOMBINANT PROTEINS; TRANSFECTION;

EID: 0035800850     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M103747200     Document Type: Article

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