Recent perspectives on the molecular structure and regulation of the beta 2-adrenoceptor.

Journal Article (Journal Article;Review)

The recent cloning of the beta 2-AR and other members of the adrenergic receptor family and related molecules has generated a flood of new information about the structure of this ubiquitous class of receptor molecules, and the ways in which their unique structures determine their function. Agonists interact with the receptor-binding pocket and somehow trigger conformational changes in the cytoplasmic portions of the receptor. These intracellular changes are then transmitted to the G-protein alpha-subunit. Phosphorylation of the receptor by several protein kinases and subsequent binding of additional cytosolic factors appear to be a major step in the control of receptor function. Changes in receptor gene expression which regulate receptor number and responsiveness provide another means to regulate transmembrance signalling. The realization that G-protein-coupled receptors are transcriptionally regulated by their own second messengers indicates that the parallels among the various members of this receptor family extend beyond their structural homologies, of 7 transmembrane segments and G-protein coupling, to include the genetic aspects of their regulation.

Full Text

Duke Authors

Cited Authors

  • Collins, S

Published Date

  • 1993

Published In

Volume / Issue

  • 52 / 26

Start / End Page

  • 2083 - 2091

PubMed ID

  • 8389951

International Standard Serial Number (ISSN)

  • 0024-3205

Digital Object Identifier (DOI)

  • 10.1016/0024-3205(93)90723-g


  • eng

Conference Location

  • Netherlands