AI Article Synopsis
- GPCRs are crucial drug targets involved in various physiological processes, making their study essential for medical advancements.
- Recent advances in structural biology have allowed scientists to observe GPCRs in detail, revealing how they function as allosteric machines that change shape in response to ligand binding.
- Understanding these conformational changes is key to grasping how GPCR activation leads to cellular responses through the action of effector proteins like G proteins and arrestins.
Article Abstract
G protein-coupled receptors (GPCRs), which mediate processes as diverse as olfaction and maintenance of metabolic homeostasis, have become the single most effective class of therapeutic drug targets. As a result, understanding the molecular basis for their activity is of paramount importance. Recent technological advances have made GPCR structural biology increasingly tractable, offering views of these receptors in unprecedented atomic detail. Structural and biophysical data have shown that GPCRs function as complex allosteric machines, communicating ligand-binding events through conformational change. Changes in receptor conformation lead to activation of effector proteins, such as G proteins and arrestins, which are themselves conformational switches. Here, we review how structural biology has illuminated the agonist-induced cascade of conformational changes that culminate in a cellular response to GPCR activation.
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| http://dx.doi.org/10.1146/annurev-biophys-070317-032931 | DOI Listing |
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