Abstract
Allosteric modulators of G-protein-coupled receptors (GPCRs) are of great pharmaceutical interest, but designing such drugs has proved challenging because the structural mechanisms by which they might act have remained unclear. Using atomic-level simulations and complementary experimental methods, we determine how a variety of allosteric modulators ligands bind to GPCRs, achieve selectivity, and control GPCR function. These findings enable the design of allosteric modulators with desired pharmacological properties.
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