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. 2021 Jul 1;12:4074. doi: 10.1038/s41467-021-24367-3

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — a 3D reconstruction of the 1:1 c-MET I/HGF I complex after focused 3D refinement of holo-complex, and the corresponding ribbon representation of this complex fitted into the cryo-EM map at 4.5 Å resolution. b The ribbon representation of the c-MET I/HGF I complex shown in side and top views. Four distinct interfaces that are involved in the interaction between c-MET I and HGF I are indicated by dash boxes. Heparin is shown in yellow as a stick model. c–e Close-up views of interfaces I, II, and III. The HGF and c-MET residues mutated for cell-based activity assays are indicated by rectangular boxes. f The levels of c-MET autophosphorylation in response to HGF wild-type (WT) or indicated mutants that were expected to disrupt c-MET I/HGF I interaction. Mean ± SEM are from N = 3 independent biological repeats. The representative raw western blot data were shown in Supplementary Fig. 5. g HGF-induced c-MET autophosphorylation in H1299 cells expressing c-MET WT or indicated mutants that were expected to disrupt C-MET I/HGF I interaction. Mean ± SEM are from N = 5 independent biological repeats. The representative western blot data were shown in Supplementary Fig. 6. h SDS-PAGE of TSE pull-down binding assay. TSI tagged c-MET927 was immobilized to TSE resin as bait and incubated with HGF WT and various of mutations as prays. i Quantification of the pull-down binding results for the HGF R242E/K244E/R249E, W321R/E361R/Y376A, and Y673A mutants shown in h. Mean ± SEM are from N = 3 independent biological repeats. Statistical difference in f, g, and i 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 f from left to right: <0.0001, 0.0124, 0.0083, <0.0001, 0.0021, 0.0251, 0.0184, 0.0361, 0.0020, 0.0284, 0.9957, 0.9414, 0.4498, 0.0038, 0.0013, <0.0001, <0.0001. Exact P values in g from left to right: <0.0001, 0.0042. Exact P values in i from left to right: 0.0353, 0.0424, 0.0006.