Fig. 2: Recognition of Aβ42 at FPR2.
From: Structural basis of FPR2 in recognition of Aβ42 and neuroprotection by humanin
a Binding pocket for Aβ42 in FPR2. The Aβ42–FPR2–Gi2 structure is shown in both side (left) and extracellular (right) views. Aβ42 is shown as sticks and colored magenta (N-terminal part) and pink (C-terminal part). b Inhibition of WK(FITC)YMVm binding to wild-type FPR2 by Aβ42, Aβ40, or Aβ1–12. Data are displayed as mean ± SEM from at least three independent experiments (n) performed in triplicate (Aβ42, n = 18; Aβ40 and Aβ1–12, n = 3). Source data are provided as a Source Data file. c–e, Interactions between FPR2 and Aβ42. Aβ42 residues and the receptor residues that are involved in interactions are shown as sticks. Polar interactions are shown as red dashed lines. c Interactions between FPR2 and the Aβ42 residues D1–E3. d Interactions between FPR2 and the Aβ42 residues E3–R5. e Interactions between FPR2 and the Aβ42 residues R5–Y10.
