Fig. 4: Cryo-EM structures of BQ3020–ETB–miniGs/q–Nb35, ET1–ETB–miniGs/q–Nb35, and ET1–ETA–miniGs/q–Nb35 complexes. | Cell Discovery

Fig. 4: Cryo-EM structures of BQ3020–ETB–miniGs/q–Nb35, ET1–ETB–miniGs/q–Nb35, and ET1–ETA–miniGs/q–Nb35 complexes.

From: Structural basis of antagonist selectivity in endothelin receptors

Fig. 4

a–c Cryo-EM density maps of ET1–ETA–miniGs/q–Nb35 (a), ET1–ETB–miniGs/q–Nb35 (b), and BQ3020–ETB–miniGs/q–Nb35 (c) complexes. d Structural comparison of ETB bound to BQ3020, IRL1620, and ET-1. Conformational comparison between BQ3020 and IRL1620 in the binding pocket (upper right), and between BQ3020 and ET-1 (bottom right). The arrow indicates that the α-helix in the binding pocket shifts slightly downward. e Sequence alignment of peptides including ET-1, BQ3020 and IRL1620. f Cross-section of the BQ3020-binding pocket in ETB. BQ3020 is displayed as spheres (left panel). Detailed interactions between BQ3020 and ETB are shown (right panel).

Back to article page