Mapping of β‐adrenoceptor coupling domains to Gs‐protein by site‐specific synthetic peptides

FEBS Letters

Palm, Dieter¹  Dees, Christian¹  Münch, Gerald¹  Hekman, Mirko¹ 

[1] Dept of Physiological Chemistry, University of Würzburg, Koellikerstraße 2, D-8700 Würzburg, FRG

关键词: Adrenoceptor;    β-;    Gs-protein;    Coupling domain;    Synthetic peptide;    Gs-protein;    guanine nucleotide-binding protein mediating stimulation of adenylate cyclase;    GTPγS;    guanosine-5′-O-(3-thiotriphosphate);    DTT;    1;    4-dithiothreitol;    NMP;    N-methylpyrrolidone;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/0014-5793(89)81015-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Peptides corresponding to the known sequence of turkey erythrocyte β₁-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.

【 授权许可】

Unknown