Journal
ANNUAL REVIEW OF PHARMACOLOGY AND TOXICOLOGY
Volume 48, Issue -, Pages 107-141Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.pharmtox.48.113006.094630
Keywords
signal transduction; receptor pharmacology; protein dynamics; protein conformation; allostery
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Funding
- NATIONAL EYE INSTITUTE [R00EY018085, T32EY007157, K99EY018085, R01EY008061] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM079191] Funding Source: NIH RePORTER
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Transformation of G protein-coupled receptors (GPCRs) from a quiescent to an active state initiates signal transduction. All GPCRs share a common architecture comprising seven transmembrane-spanning a-helices, which accommodates signal propagation from a diverse repertoire of external stimuli across biological membranes to a heterotrimeric G protein. Signal propagation through the transmembrane helices likely involves mechanistic features common to all GPCRs. The structure of the light receptor rhodopsin may serve as a prototype for the transmembrane architecture of GPCRs. Early biochemical, biophysical, and pharmacological studies led to the conceptualization of receptor activation based on the context of two-state equilibrium models and conformational changes in protein structure. More recent studies indicate a need to move beyond these classical paradigms and to consider additional aspects of the molecular character of GPCRs, such as the oligomerization and dynamics of the receptor.
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