Fig. 7

Key domains and amino acid residues of LILRB2 for ligands and antibody binding. a. Schematic diagram showing the design of domain-swapping mutants of LILRB2. B1D1 and B1D2 mutants were generated by replacing the D1 and D2 domains of LILRB2 with their corresponding domains from LILRB1, respectively. b-d. oAβ, PS, and Ab29 binding to LILRB2 mutants as measured on chimeric reporter cells. Chimeric NFAT-GFP reporter cells expressing individual mutants of LILRB2 (listed in x-axis) were incubated with oAβ (b) PS (c), and Ab29 (d). The activation of reporter cells is shown as the percentage of GFP⁺ cells. Data are presented as mean ± SD (n = 3 independent experiments). e. Alignment of D1 and D2 domains of LILRB2 and LILRB1. Amino acid residues are numbered according to Uniprot entry Q8N423. Identical residues are shown in white text with red background. Similar residues are shown in black text with a yellow background. Non-conserved residues are in white background. Individual domains of LILRB2 are also labeled. The red arrows indicate the single-amino acid mutations designed for testing. f. Crystal structure of LILRB2 (2gw5) visualized in UCSF Chimera showing the D1 and D2 domains as ribbons. Selected residues for mutation studies are shown in ball-and-stick with side chains displayed. Three-letter code names and residue numbers are also labeled following Uniprot entry Q8N423. g. Schematic diagram showing the distribution of single-amino acid mutations in LILRB2 D1 and D2 domains