Mapping of beta-adrenoceptor coupling domains to Gs-protein by site-specific synthetic peptides.
Peptides corresponding to the known sequence of turkey erythrocyte beta 1-adrenergic receptor were synthesized and the effects on receptor-mediated cyclase activation were measured. Peptides corresponding to the first and second intracellular loops (T61-71 and T138-159) inhibited at micromolar concentrations the hormone-dependent cyclase activation in turkey erythrocyte membranes. In contrast, the peptide corresponding to the C-terminal part of the third intracellular loop (T284-295) increased the cyclase activity in a hormone-independent manner. Peptides T338-353 and T2-10 and a number of synthetic peptides unrelated to the beta-adrenoceptor had no effect.
Palm
D
D
Dept of Physiological Chemistry, University of Würzburg, FRG.
Münch
G
G
Dees
C
C
Hekman
M
M
D000262:Adenylyl Cyclases / Q000032:analysis*; D000818:Animals; D001665:Binding Sites; D004789:Enzyme Activation / Q000187:drug effects; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000032:analysis*; D006160:Guanosine Triphosphate / Q000494:pharmacology; D007545:Isoproterenol / Q000494:pharmacology; D015394:Molecular Structure; D010449:Peptide Mapping; D010455:Peptides / Q000138:chemical synthesis; D011433:Propranolol / Q000494:pharmacology; D011943:Receptors, Adrenergic, beta / Q000032:analysis* / Q000502:physiology; D014422:Turkeys
D010455:Peptides; D011943:Receptors, Adrenergic, beta; D006160:Guanosine Triphosphate; D011433:Propranolol; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases; D007545:Isoproterenol