Journal
TRENDS IN PHARMACOLOGICAL SCIENCES
Volume 28, Issue 8, Pages 397-406Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tips.2007.06.003
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Funding
- NINDS NIH HHS [R37NS28471] Funding Source: Medline
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G-protein-coupled receptors (GPCRs) are remarkably versatile signaling molecules. Members of this large family of membrane proteins respond to structurally diverse ligands and mediate most transmembrane signal transduction in response to hormones and neurotransmitters, and in response to the senses of sight, smell and taste. Individual GPCRs can signal through several G-protein subtypes and through G-protein-independent pathways, often in a ligand-specific manner. This functional plasticity can be attributed to structural flexibility of GPCRs and the ability of ligands to induce or to stabilize ligand-specific conformations. Here, we review what has been learned about the dynamic nature of the structure and mechanism of GPCR activation, primarily focusing on spectroscopic studies of purified human beta(2) adrenergic receptor.
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