Abstract
Structural Biology G protein–coupled receptors (GPCRs) are responsible for transducing diverse signals from outside to inside cells. This process requires specificity both in ligand binding to GPCRs and in coupling between GPCRs and their intracellular partners, G proteins. Qiao et al. determined the structure of the human glucagon receptor (GCGR), a type B GPCR, bound to glucagon and one of two heterotrimeric G proteins, Gs or Gi1. GCGR signals mainly through Gs, and the structures provide a basis for this specificity. Conformational changes in GCGR, relative to the inactive state, create a binding cavity for the G proteins. The pocket is opened sufficiently to accommodate a bulky binding motif in Gs. Gi1 can still bind but the pocket does not close around it, so there is a smaller interaction interface. Science , this issue p. [1346][1] [1]: /lookup/doi/10.1126/science.aaz5346
Published Version
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