Fig. 2: Characterization of macitentan, ambrisentan, and zibotentan binding modes in ETA.
From: Structural basis of antagonist selectivity in endothelin receptors
a–d Schematic of macitentan’s interactions with key residues in ETA. e–h Schematic of ambrisentan’s interactions with key residues in ETA. i–l Schematic of zibotentan’s interactions with key residues in ETA. The selectivity of zibotentan towards ETA may be attributed to Y1292.53 in ETA but H1502.53 in ETB (l). m–o The antagonistic effects of four different antagonists on the ETA R3266.55A variant (m); effects of mutations in ETA (n) and ETB (o) on zibotentan’s antagonistic activity. ΔpIC50 represents the difference in pIC50 values between the wild type (WT) and the mutants of ETA. Data are presented as means ± SEM (n ≥ 3). Hydrogen bonds are highlighted with gray dashed lines.
