The conformational change responsible for AT1 receptor activation is dependent upon two juxtaposed asparagine residues on transmembrane helices III and VII

Journal of Biological Chemistry

Volumn 272, Issue 7, 1997, Pages 4245-4251

  Balmforth, Anthony J ^a   Lee, Alison J ^a   Warburton, Philip ^a   Donnelly, Dan ^a   Ball, Stephen G ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOTENSIN; ANGIOTENSIN 1 RECEPTOR; ANGIOTENSIN DERIVATIVE; ASPARAGINE; INOSITOL TRISPHOSPHATE; MUTANT PROTEIN; SERINE;

ARTICLE; CARDIOVASCULAR EFFECT; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; HUMAN; HUMAN CELL; LIGAND BINDING; PHOSPHOINOSITIDE METABOLISM; PRIORITY JOURNAL; PROTEIN CONFORMATION; RECEPTOR AFFINITY; RENIN ANGIOTENSIN ALDOSTERONE SYSTEM; SITE DIRECTED MUTAGENESIS;

ALANINE; AMINO ACID SEQUENCE; ANGIOTENSIN I; ANIMALS; ASPARAGINE; CELL LINE; HUMANS; INOSITOL 1,4,5-TRISPHOSPHATE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RATS; RECEPTORS, ANGIOTENSIN; SEQUENCE HOMOLOGY, AMINO ACID; SERINE; TRANSFECTION;

EID: 0031041454     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.7.4245     Document Type: Article

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