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. 2019 Oct 2;9:14159. doi: 10.1038/s41598-019-50335-5

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© The Author(s) 2019

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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Chemoproteomic analysis of the JAK kinase family. (a) Overview of the domain organization of the JAK family. Two kinase domains are present in all members of this kinase family. (b) Chemical structure of capturing compound 15 used to enrich all JAK family members via their active kinase domain. (c) Determination of apparent pK_ds using a chemoproteomic workflow with antibody readout for the marketed kinase inhibitor tofacitinib 17 (which only binds to the second (active) kinase domain). Capturing tool was either the new kinobeads mix, or 15. (d) Chemical structures of all JAK family inhibitors used in this study. (e) Tanimoto similarities for the structures from. (d,f) Determination of apparent dissociation constants of 11 JAK kinase family inhibitors for the JAK kinase family.