Fig. 1: Cryo-EM structure of the PACAP27–VIP2R–Gs complex.
From: A distinctive ligand recognition mechanism by the human vasoactive intestinal polypeptide receptor 2
a Binding specificity of PACAP and VIP receptor subfamily to the related peptide hormones. Sequence alignment of peptides is shown on the top panel. b Receptor signaling profiles of endogenous agonists PACAP27, PACAP38, and VIP. Data shown are means ± S.E.M. of at least three independent experiments performed in quadruplicate (n = 3–6). Source data are provided as a Source Data file. c Cut-through view of the cryo-EM density map illustrating the PACAP27–N-terminal modified VIP2R(24-438)–Gs complex and the disc-shaped micelle. d Model of the PACAP27–N-terminal modified VIP2R(24-438)–Gs complex as a cartoon, with PACAP27 as helix in orange. The receptor is shown in green, Gαs in yellow, Gβ subunit in royal blue, Gγ subunit in violet, and Nb35 in gray. e Cut-through view of the cryo-EM density map illustrating the PACAP27–VIP2R(1-438)–Gs complex and the disc-shaped micelle. f Model of the PACAP27–VIP2R(1-438)–Gs complex as a cartoon, with PACAP27 as helix in gold. The receptor is shown in light green, Gαs in yellow, Gβ subunit in royal blue, Gγ subunit in violet, and Nb35 in gray.
