Fig. 5

p. L191S mutation reduces the binding ability of FGF5 to FGFR1. a Structure prediction of FGF5. The three-dimensional structure of the FGF5 protein was predicted by I-TASSER based on its homologue, FGF1 (PDB ID: 3OJV). The predicted structure of FGF5 was visualized by PyMOL and shown as a ribbon diagram. The interactions between the side chains of L191 and S211 are magnified. b Evaluation of the effect of p. L191S mutation on the interaction between FGF5 and FGFR1. HEK293T cells were co-transfected with FGFR1 and FGF5-Flag or mu-FGF5-Flag plasmids. At 48 h after transfection, the cells were lysed with IP lysis buffer, followed by IP with anti-Flag IP resin. The input and IP products were subjected to immunoblotting with antibodies against FGFR1, Flag and tubulin. c Densitometry analysis of the digital immunoblotting images including Panel b and others of repeated tests. Relative fold changes in FGFR1 levels in IP products are shown after normalization to the corresponding FGF5 or mu-FGF5 level. Error bars represent standard errors of the repeated experiments. Significant differences between the two groups were calculated by Student’s t test, * represents p < 0.05