Mapping of beta-adrenoceptor coupling domains to Gs-protein by site-specific synthetic peptides.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Palm D,Münch G,Dees C,Hekman M

doi

10.1016/0014-5793(89)81015-4

subject

Has Abstract

pub_date

1989-08-28 00:00:00

pages

89-93

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(89)81015-4

journal_volume

254

pub_type

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