Conservation of putative collagen-binding residues in LAIR-1 and GPVI. (Left) Surface representations of the LAIR1-CBD (A) and the GPVI ectodomain (D) showing in blue residues that contribute to collagen binding according to mutagenesis data, in red residues that form the LAIR-1 collagen binding surface based on the NMR titrations, and in green residues that contact docked collagen peptides in GPVI. Data for LAIR-1 and GPVI are from this study and Horii et al,¹⁴  respectively. GPVI residues, L53 and F54 that are part of the docking interface as well as the equivalent of the LAIR-1/collagen interface, are shown in green. (Right) Surface representations in 2 orientations of LAIR-1 (B-C) and GPVI (E) showing in red residues that are strictly conserved within the LAIR-family (B), within both the LAIR and GPVI families (C) and, residues conserved within the GPVI family only (E). Note that putative collagen-binding residues of LAIR-1 are significantly conserved in both LAIR and GPVI families, whereas putative collagen-binding residues of GPVI are not at all conserved. Conservation is based on the alignments shown in supplemental Figures 5 and 6. The orientation of LAIR is identical to Figure 2B, whereas GPVI is depicted with its D1 domain in an orientation similar to LAIR-1.