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. 2021 Mar 6;14:40. doi: 10.1186/s13045-021-01049-7

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© The Author(s) 2021

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 — Mechanisms for the action of representative BTK inhibitors. a Chemical structure of the covalent BTK inhibitor ibrutinib. b Chemical structure of the non-covalent BTK inhibitor ARQ 531. c Ibrutinib covalently binds to BTK cysteine 481 (C481), competes with ATP in the ATP binding pocket, and inhibits autophosphorylation of BTK. The action of ibrutinib requires its binding to BTK C481, and BTK C481 mutations abrogate the binding of ibrutinib and lead to the resistance to ibrutinib. d ARQ 531 non-covalently interacts with BTK, occupies the ATP binding pocket, and inhibits BTK autophosphorylation. The effect of ARQ 531 does not require its binding to BTK C481. Therefore, ARQ 531 remains active in patients with BTK C481 mutations. c, d were made by using PyMOL 0.99