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Molecular basis for high-affinity agonist binding in GPCRs

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Science  24 May 2019:
Vol. 364, Issue 6442, pp. 775-778
DOI: 10.1126/science.aau5595

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A GPCR seen in the active state

G protein–coupled receptors (GPCRs) are exceptionally good targets for drug development. Warne et al. describe four crystal structures of complexes of a GPCR—the β1-adrenergic receptor—in its active state. They used nanobodies (recombinant variable domains of heavy-chain antibodies) and engineered G protein to stabilize the β1-adrenergic receptor bound to a full agonist, two partial agonists, and a weak partial agonist. Comparison of these structures to the inactive state elucidates how agonist binding is altered in the active conformation.

Science, this issue p. 775