Extended Data Fig. 3: Electron microscopy density map of C48/80–MRGPRX2–Gi1 and PAMP-12–MRGPRX2-Gi1 complex.
From: Structure, function and pharmacology of human itch receptor complexes
a-d, EM density of the TM helices of MRGPRX2 and the α5 helix of Gαi1 of C 48/80–MRGPRX2–Gi1 (a), PAMP-12–MRGPRX2–Gi1 (b), C14linear–MRGPRX2–Gi1 complex (c) and SP–MRGPRX2–Gi1 complex (d) respectively. All seven-TM bundles were unambiguously traceable in the cryo-EM density map, and the densities of large hydrophobic residues were utilized to assign the primary sequence of MRGPRX2. e, Position of ligand-binding pockets in the C14linear–MRGPRX2–Gi1, SP–MRGPRX2–Gi1, β2AR–Gs (PDB: 3SN6), CB1–Gi (PDB: 6N4B), μ-opioid–Gi (PDB: 6DDF) and GPR97–mGo (PDB: 7D76) complex. The distance between ligand and “toggle switch” were shown. f, Dose response curves of the C48/80, PAMP-12, C14linear and SP induced Gαq–Gγ dissociation in MRGPRX2 overexpressing cells. Data from three independent experiments are presented as the mean ± SEM (n=3). All data were analysed by two-sided one-way ANOVA with Turkey test.
