A mutation of the beta 2-adrenergic receptor impairs agonist activation of adenylyl cyclase without affecting high affinity agonist binding. Distinct molecular determinants of the receptor are involved in physical coupling to and functional activation of Gs.
Open Access
- 1 January 1990
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 265 (3), 1388-1393
- https://doi.org/10.1016/s0021-9258(19)40026-4
Abstract
No abstract availableThis publication has 28 references indexed in Scilit:
- Structure of the Adrenergic and Related ReceptorsAnnual Review of Neuroscience, 1989
- From Epinephrine to Cyclic AMPScience, 1988
- Roles of G protein subunits in transmembrane signallingNature, 1988
- Identification of residues required for ligand binding to the beta-adrenergic receptor.Proceedings of the National Academy of Sciences, 1987
- G PROTEINS: TRANSDUCERS OF RECEPTOR-GENERATED SIGNALSAnnual Review of Biochemistry, 1987
- The carboxyl terminus of the hamster β-adrenergic receptor expressed in mouse L cells is not required for receptor sequestrationCell, 1987
- Ligand binding to the β-adrenergic receptor involves its rhodopsin-like coreNature, 1987
- [71] Use of eukaryotic expression technology in the functional analysis of cloned genesMethods in Enzymology, 1987
- Regression analysis of nonlinear Arrhenius plots: An empirical model and a computer programComputers in Biology and Medicine, 1984
- A highly sensitive adenylate cyclase assayAnalytical Biochemistry, 1974