Fig. 2: Gi-coupled ETBR is in an active conformation.
From: Structure of endothelin ETB receptor–Gi complex in a conformation stabilized by unique NPxxL motif
a Superposition of the Gi-bound ETBR structure (green) with the partially active-state crystal structure of ET-1-bound ETBR (blue) and the inactive-state crystal structure of the antagonist bosentan-bound ETBR (magenta). b–e Close-up views of conserved motifs involved in receptor activation. Arrows indicate the repositioning of side chains from the inactive to active state. f, g Concentration–response curves for ET-1-induced Gi signaling activity in the NanoBiT G-protein dissociation assay of ETBR–wild-type (WT) and mutant receptors. Symbols and error bars represent mean and standard error of the mean (SEM), respectively, from three independent experiments, each performed in duplicate or triplicate. Signaling of reduced amounts of WT ETBR (% of plasmid DNA transfected) for Gi is shown in gray. Data for these figures and expression levels of WT and mutant receptors measured by [125I]ET-1 binding are shown in Supplementary Fig. 8 and Table 1a, b.
