Fig. 4: Structural differences between FPR1 and FPR2. | Nature Communications

Fig. 4: Structural differences between FPR1 and FPR2.

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

Fig. 4

a Dose-dependent action of fMLFII on wide type FPR1 (wtFPR1) and FPR1 with mutations of three non-conserved residues to their counterparts in FPR2. 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. b Charge distributions of fMLFII-binding pockets in FPR1 and FPR2. Overall binding modes of fMLFII in FPR1 (blue) and FPR2 (slate). c Alignment of the extracellular regions of FPR1 and FPR2 showing different conformations of ECL2 and ECL3. Two non-conserved residues, S84 and D283 in FPR2 (slate) and R84 and G280 in FPR1 (blue), are shown as sticks. d Structural comparison of the extracellular surfaces of FPR1 and FPR2. fMLFII is colored orange in FPR2 and yellow in FPR1. ECL extracellular loop.

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