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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. 6 — a 3D reconstruction of the 2:2 c-MET/NK1 complex, and the corresponding ribbon representation of this complex fitted into the cryo-EM map at 5 Å resolution, shown in two orthogonal views. b The ribbon representation of the 2:2 c-MET/NK1 complex shown in two orthogonal views. c Close-up view of the interface between c-MET-SEMA and HGF-K1, showing in two views. d Superposition between free NK1 dimer (PDB ID: 1NK1⁴⁴; white) and NK1 dimer after binding c-MET (colored). e The levels of c-MET autophosphorylation in response to NK1 or NK2. Mean ± SEM are from N = 3 independent biological repeats. Statistical difference was analyzed using two-tailed Student’s t-test and P values were calculated between WT and mutants: **P ≤ 0.01; ***P ≤ 0.001. The representative western blot data were shown in Supplementary Fig. 5. Source data are provided as a Source Data file. Exact P values in e from left to right: 0.0043, <0.0001.