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. 2016 Sep 2;9:80. doi: 10.1186/s13045-016-0313-y

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© The Author(s). 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 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.

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Fig. 1 — The structure of Bruton tyrosine kinase (BTK). BTK has a pleckstrin-homology (PH) domain, SH3 and SH2 (src-homology) domains, and a kinase domain. The BTK polypeptide has 659 amino acid residues with an approximate molecular weight of 76 kDa. The C481S mutation in the kinase domain mediates resistance to ibrutinib