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. 2016 Jan 26;17(2):128–136. doi: 10.1038/tpj.2015.97

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Copyright © 2016 Macmillan Publishers Limited

This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/4.0/

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Structural view of protein–drug interactions. (a) Superposition (c-alpha atoms) of imatinib binding to eight target protein X-ray structures (ABL1, LCK, KIT, NQO2, ABL2, SYK, DDR1 and MAPK14). The superimposed protein structures are colored. The blue to red color represents low to high conservation. The ligand is shown bound to protein pockets. (b) Imatinib binding to the same target proteins as shown in (a). Only the side chains of binding sites are shown. (c) Imatinib binding to its target proteins. The side chains of proteins are imatinib binding sites that are mutated.