Fig. 6: Binding of C43 to FPR2.

a Details of C43-binding pocket. FPR2 and C43 are colored in light green and purple, respectively. Polar interactions are shown as black dashed lines. b Ligplot schematic representation of C43 interactions with FPR2. The carbon, nitrogen, oxygen, and sulfur atoms are colored in black, blue, red, and yellow, respectively. Residues in FPR2 that form polar interactions with C43 are shown with green labels. Polar interactions are shown as green dashed lines. c Dose-dependent action of C43 on wide type FPR2 (wtFPR2) and mutants measured by cAMP accumulation assay. Each data point represents mean ± S.D. Three independent assays were performed. d Structural alignment of FPR2 bound to four agonists. The chlorophenyl group of C43 overlaps with the terminal methionine residues in three peptide agonists in the activation chamber. e Conserved agonist-binding mechanism for FPR1 and FPR2. For a particular agonist, it sticks into the activation chamber to cause conformational changes of V^3.40, W^6.48, P^5.50, and F^6.44 to activate receptors. This is facilitated by a polar interaction network with D^3.33, R^5.42, and R^5.38 at the mouth region. Above the mouth region, the vase space of agonist-binding pocket may tolerate a large chemical diversity. Source data are provided as a Source Data file.