Yaozhong Zou

TL;DR: This crystal structure represents the first high-resolution view of transmembrane signalling by a GPCR and the most surprising observation is a major displacement of the α-helical domain of Gαs relative to the Ras-like GTPase domain.

TL;DR: NMR spectroscopy is used to characterize the conformational dynamics of the transmembrane core of the β(2)-adrenergic receptor (β(2)AR), a prototypical GPCR, and shows that for β( 2)AR, unlike rhodopsin, an agonist alone does not stabilize a fully active conformation.

TL;DR: NMR spectroscopy is used to demonstrate conformational coupling between the ECS and the orthosteric binding site, showing that drugs targeting this diverse surface could function as allosteric modulators with high subtype selectivity.

TL;DR: In this paper, NMR spectroscopy was used to characterize the conformational dynamics of the transmembrane core of the b2-adrenergic receptor (b2AR), a prototypical GPCR.

TL;DR: The active-state structure of a GPCR occupied by a partial agonist, β2AR with salmeterol, together with mutagenesis and biophysical studies, explains this ligand's unusual pharmacological profile.