Abstract
Allosteric signaling in G-protein-coupled receptors (GPCRs) involve binding of a ligand in the extracellular region which induces conformational changes in the intracellular part and coupling to G proteins. This triggers a cascade of signaling that results in cellular responses. Therefore, to design drugs that modulate the GPCR function, there is an urgent need to understand the conformational pathways in GPCR activation and inactivation and their dynamical behavior. Importantly, the atomic details of the allosteric pathway between the active site and the ligand binding site can help design better drugs that can disrupt or induce specific allosteric pathways.
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