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. 2021 Jul 9;12:4226. doi: 10.1038/s41467-021-24291-6

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Fig. 2 — a Conformational change on LAIR1 c-c’ loop to enable RIFIN binding. b Alignment of LAIR1 sequences. (MGD21, hLAIR1: native human LAIR1, MGJ5, MGB47, MGC34, gLAIR1: gorilla LAIR1). c Accumulation of critical mutations allows affinity maturation of LAIR1 to RIFIN (upper left panel: SDS-PAGE image; lower left: LAIR1 de-glycosylation by EndoH; upper right panel: SDS-PAGE sample loading list; lower right panel: Quantification of left panel by bar graph. Data are presented as mean values ± SD). n = 3 independent measurements. The SDS-PAGE runs were repeated at least twice. d RIFIN binding footprint overlapped that of collagen on LAIR1 surface. Note: LAIR1 residue numbering is based on MGD21 construct, which has 84 shift to that of native LAIR1.