Fig. 3: Binding of fMLFII to FPR1 and FPR2. | Nature Communications

Fig. 3: Binding of fMLFII to FPR1 and FPR2.

From: Molecular recognition of formylpeptides and diverse agonists by the formylpeptide receptors FPR1 and FPR2

Fig. 3

a Overall binding modes of fMLFII in FPR1 (blue) and FPR2 (slate). The N-terminal formyl methionine residue of fMLFII is circled. b Details of binding pockets of fMLFII in FPR2 (left) and FPR1 (right). Red arrows point to non-conserved residues H102 and F257 in FPR2 and F102 and Y257 in FPR1. Polar interactions are shown as black dashed lines. The activation chamber is shown between the two purple dashed lines. c Ligplot schematic representation of fMLFII interactions with FPR2 (left) and FPR2 (right). The carbon, nitrogen, oxygen, and sulfur atoms are colored in black, blue, red, and yellow, respectively. Residues in FPR1 and FPR2 that form polar interactions with fMLFII are shown with green labels. Polar interactions are shown as green dashed lines. The ligand is shown as purple sticks. d Dose-dependent action of fMLFII on wide type FPR1 (wtFPR1) and mutants. Agonist-induced FPR1 signaling was measured by cAMP accumulation assay. Each data point represents mean ± S.D. Three independent assays were performed. Source data are provided as a Source Data file.

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