Fig. 3: Interface between c-MET II and HGF I.

a 3D reconstruction of the c-MET II/HGF I/HGF II sub-complex and the corresponding ribbon representation of this complex fitted into a cryo-EM map of sub-complex at 4 Å resolution. b The ribbon representation of the c-MET II/HGF I/HGF II complex shown in side and top views. c Detailed view of the c-MET II-SEMA/HGF I-K1 interface shown in two different views. The HGF and c-MET residues mutated for cell-based activity assays are indicated by rectangular boxes. d The levels of c-MET autophosphorylation in response to HGF wild-type (WT) or indicated mutants that were expected to disrupt c-MET II/HGF I interaction. Mean ± SEM are from N = 3 independent biological repeats. The representative western blot data were shown in Supplementary Fig. 5. e HGF-induced c-MET autophosphorylation in H1299 cells expressing c-MET WT or indicated mutants that were expected to disrupt C-MET II/HGF I interaction. Mean ± SEM are from N = 5 independent biological repeats. The representative western blot data were shown in Supplementary Fig. 6. f Quantification of the pull-down binding result for the HGF E159R mutant shown in Fig. 2h. Mean ± SEM are from N = 3 independent biological repeats. Statistical difference in d–f was analyzed using two-tailed Student’s t-test, and P values were calculated between WT and mutants: ns, P > 0.05; *P ≤ 0.05; **P ≤ 0.01; ***P ≤ 0.001. Source data are provided as a Source Data file. Exact P values in d from left to right: <0.0001, 0.0012, 0.0319. Exact P value in e: <0.0001. Exact P value in f: 0.0002.