Abstract
G protein-coupled receptors (GPCRs) include various neurotransmitters and hormones, and over 30% of modern drugs target GPCRs. The number of GPCR crystal structures has rapidly increased, and many structures of GPCRs in complexes with their binding partners are being solved by cryo-electron microscopy. However, crystallographic or cryo-electron microscopy data alone cannot fully explain the important features of GPCR signaling determined experimentally. Recent studies have suggested that GPCRs are structurally dynamic, and exchange between multiple conformations. In this respect, NMR methods provide information about the dynamics of proteins over a wide range of frequencies, in aqueous solutions at nearphysiological temperatures. Although NMR studies of GPCRs are challenging due to their innate instability and relatively large molecular weights, recent methodological advances have enabled us to observe the NMR signals of various GPCRs. These NMR studies revealed that GPCRs exist in function-related equilibria between locally different conformations that are simultaneously populated. Here we will describe solution NMR studies that have clarified the function-related conformational dynamics of two GPCRs, β2 adrenergic receptor and adenosine A2A receptor.
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