Abstract
G-protein-coupled receptors (GPCRs) mediate a wide range of cellular responses to various ligands or stimuli, and are the most important drug targets associated with human diseases. While major advances in GPCR structural biology have greatly deepened our understanding of its activation mechanism, the highly complex changes in the structural dynamics of GPCRs during activation remain underdetermined and their links to physiological functions largely unknown. Solution nuclear magnetic resonance (NMR) spectroscopy is an essential technique that allows the characterization of protein structural dynamics at atomic level, and has been applied in the studies of GPCR structural-function relationship in the past decade. Herein, we summarize a few specific studies in which solution NMR methods were employed and provided novel insights into questions difficult to be addressed by other methods.
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