Fig. 3: Comparison of the binding mode of PACAPs to VIP1R and PAC1R. | Nature Communications

Fig. 3: Comparison of the binding mode of PACAPs to VIP1R and PAC1R.

From: Cryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy

Fig. 3

a Sequence alignment of the VIP1R peptide ligands VIP, PACAP27, and PACAP38. b The binding mode of PACAP27 to VIP1R, showing that PACAP27 adopts α-helical conformation and interacts with all TM helices of VIP1R except TM4. c The cross-section view of the PACAP27 binding pocket in the TM bundle of VIP1R. Structural comparisons of PACAP binding pockets in VIP1R and PAC1R. Residues interact with peptide amino acids H1 and D3 (d), S2 (e), G4, I5, and F6 (f), as well as amino acids from T7 to R14 (g, h) are shown as sticks. The hydrogen bonds between PACAP27 and residues of VIP1R are marked as black dotted lines, and the hydrogen bonds between PACAP38 and residues of VIP1R are shown as red dotted lines. PACAP27 is colored in orange, and VIP1R in green. PACAP38 is shown in cyan, and PAC1R (PDB code: 6P9Y) in light blue.

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