Fig. 3: Interactions between FPR2 and fHN.
From: Structural basis of FPR2 in recognition of Aβ42 and neuroprotection by humanin
a Comparison of fHN- and Aβ42-binding sites in FPR2. The peptides fHN and Aβ42 are shown as green and magenta sticks, respectively. Only the receptor in the fHN–FPR2–Gi2 structure is shown in yellow cartoon representation for clarity. b, d, f Binding and cell-signaling assays of FPR2. Bars represent differences in calculated fHN-binding affinity (pKi; b, f) or potency (pEC50, d) for each mutant relative to the wild-type receptor or peptide (WT). Data are displayed as mean ± SEM (bars) from at least three independent experiments performed in triplicate with individual data points shown (dots). *P < 0.05, **P < 0.001, ***P < 0.0001 by one-way analysis of variance followed by Dunnett’s post-test compared with the response to the wild-type fHN (b) or the response of the wild-type receptor (d, f). Supplementary Tables 1, 3 provide detailed statistical evaluation, P-values, numbers of independent experiments (n), and expression levels. Source data are provided as a Source Data file. b Inhibition of WK (FITC) YMVm binding to wild-type FPR2 by fHN variants. d fHN-induced IP accumulation of FPR2 mutants. f Inhibition of WK (FITC)YMVm binding to FPR2 mutants by fHN. c, e Interactions between FPR2 and fHN. The fHN residues and the receptor residues involved in interactions are shown as sticks. Polar interactions are shown as red dashed lines. c Interactions between FPR2 and the fHN residues fM1–P3. e Interactions between FPR2 and the fHN residues R4–S14. The two hydrophobic interaction cores are highlighted by two black dashed circles.
