The sixth transmembrane domains of the human B1 and B2 bradykinin receptors are structurally compatible and involved in discriminating between subtype-selective agonists

Journal of Biological Chemistry

Volumn 272, Issue 1, 1997, Pages 311-317

  Leeb, Tosso ^a,b   Mathis, Sandra A ^a   Leeb Lundberg, L M Fredrik ^a  

^a UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

^b UNIVERSITY OF GÖTTINGEN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BRADYKININ; BRADYKININ B1 RECEPTOR; BRADYKININ B2 RECEPTOR; BRADYKININ RECEPTOR; KALLIDIN; RECEPTOR SUBTYPE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; LIGAND BINDING; MEMBRANE STRUCTURE; PRIORITY JOURNAL; PROTEIN STRUCTURE; RECEPTOR AFFINITY; RECEPTOR BINDING; SIGNAL TRANSDUCTION;

BINDING, COMPETITIVE; CELL LINE; HUMANS; LIGANDS; MEMBRANE PROTEINS; RADIOLIGAND ASSAY; RECEPTOR, BRADYKININ B1; RECEPTOR, BRADYKININ B2; RECEPTORS, BRADYKININ; RECOMBINANT FUSION PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0031027029     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.1.311     Document Type: Article

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