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Chem Rev. 2017 Jan 11;117(1):139-155. doi: 10.1021/acs.chemrev.6b00177. Epub 2016 Sep 13.

GPCR Dynamics: Structures in Motion.

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Department of Computer Science, ‡Biophysics Program, §Department of Molecular and Cellular Physiology, and ∥Institute for Computational and Mathematical Engineering, Stanford University , Stanford, California 94305, United States.


The function of G protein-coupled receptors (GPCRs)-which represent the largest class of both human membrane proteins and drug targets-depends critically on their ability to change shape, transitioning among distinct conformations. Determining the structural dynamics of GPCRs is thus essential both for understanding the physiology of these receptors and for the rational design of GPCR-targeted drugs. Here we review what is currently known about the flexibility and dynamics of GPCRs, as determined through crystallography, spectroscopy, and computer simulations. We first provide an overview of the types of motion exhibited by a GPCR and then discuss GPCR dynamics in the context of ligand binding, activation, allosteric modulation, and biased signaling. Finally, we discuss the implications of GPCR conformational plasticity for drug design.

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