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Mapping of β‐adrenoceptor coupling domains to G s ‐protein by site‐specific synthetic peptides
Author(s) -
Palm Dieter,
Münch Gerald,
Dees Christian,
Hekman Mirko
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81015-4
Subject(s) - intracellular , peptide , cyclase , chemistry , receptor , biochemistry , peptide hormone , adrenergic receptor , hormone , biophysics , biology
Peptides corresponding to the known sequence of turkey erythrocyte β 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 β‐adrenoceptor had no effect.