Research Article

Structural basis of Gs and Gi recognition by the human glucagon receptor

See allHide authors and affiliations

Science  20 Mar 2020:
Vol. 367, Issue 6484, pp. 1346-1352
DOI: 10.1126/science.aaz5346

You are currently viewing the editor's summary.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

Choosing a partner that fits

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

View Full Text

Stay Connected to Science