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. 2022 Jun 11;15:79. doi: 10.1186/s13045-022-01299-z

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© The Author(s) 2022

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 4 — Comparison of the binding models of foretinib, cabozantinib and merestinib against MET with D1228V mutation. Using MolDesk Basic ver. 1.1.77, molecular docking simulations of foretinib, cabozantinib and merestinib with the c-Met kinase domain (wild type or D1228V mutant) were carried out. Using PyMOL (ver 2.5.2), the 3D docking model of each MET-TKI and wild-type MET was aligned to the structure of MET D1228V. A The closest distances (Å) between the quinoline or pyrazole group of cabozantinib, merestinib, or foretinib and MET V1228 were measured by PyMOL. B The closest distances between the quinoline group of modified foretinib and MET V1228 were measured by PyMOL