Fig. 3: Peptidomimetic agonism and subtype selectivity demonstrated by compound 4 and DC591053.

a The cross-section view of the compound 4 binding pocket in RXFP4. b Detailed interactions of compound 4 (cyan) with residues in RXFP4 (dark sea green). c Effects of receptor mutations on compound 4-induced cAMP accumulation. Data are shown as means ± S.E.M. of at least three independent experiments. d Schematic diagram of interactions between ligands and receptor. Amino acid residues of RXFP4 are colored red for salt bridge, yellow for hydrogen bond, green for π-π stacking and gray for hydrophobic interactions. Different residues around the binding pocket in RXFP3 and RXFP4 are highlighted in pink. e Subtype selectivity of DC591053 at RXFP4 without observable cross-reactivity in RXFP3. Data are shown as means ± S.E.M. of three independent experiments (n = 3). f The cross-section view of the DC591053 binding pocket in RXFP4, with the RXFP4-specific edge in the ligand-binding pocket highlighted in an orange circle. g Detailed interactions of DC591053 (magenta) with residues in RXFP4 (medium purple). h Effects of receptor mutations on DC591053-induced cAMP accumulation. Data are shown as means ± S.E.M. of at least three independent experiments. The numbers of independent experiments are shown in the parentheses. Supplementary Table 4 provides detailed statistical evaluation such as P values and numbers of the independent experiment (n). Source data are provided as a Source Data file.