G-protein coupled receptors (GPCRs) are relatively large (350  residues and 7 trans-membrane helices) membrane proteins that are a dominant sigallying mechanism in cells. Their actions are complex involving the binding of agonists, G-proteins, and importantly they are the largest class of drug receptors. Their actions rely on the intrinsic platicity of the protein as modulated by binding of effector molecules. A wide range of solid-state NMR methods are used for determing the structures and describing the dynamics of GPCRs in multiple states. These include moderate and fast magic angle spinning, static and rotationally aligned, and conventional solid-state NMR methods. Recent progress on the chemokine receptors CXCR1 and CXCR2 and their interactions with the chemokine IL-8 and the cognate G-protein will be described.

NMR approaches to GPCRs in phospholipid bilayers

251st National Meeting (2016)

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