Single-particle cryo-EM structural studies of the β2AR–Gs complex bound with a full agonist formoterol

G-protein-coupled receptors (GPCRs) modulate cytoplasmic signaling in response to extracellular stimuli, and are important therapeutic targets in a wide range of diseases. Differential ligands binding to receptor promote different conformations of GPCR–G-protein complex, which can adopt diverse active states. Such ligand-directed biased agonism is now an important focus in drug discovery. Therefore, structure determination of GPCR–G-protein complexes in variable activation states is important to elucidate the mechanisms of signal transduction, and to facilitate drug discovery.