Abstract
Bruton's tyrosine kinase (BTK) plays a critical role in disorders associated with B-cell production and it is often targeted to effectively treat certain lymphomas, leukemias, and other B-cell malignancies. A widely used BTK inhibitor, namely ibrutinib, covalently binds the protein at a specific residue and renders it inactive. Unveiling the reaction mechanism of BTK inhibition by ibrutinib presents various challenges. For instance, it involves several chemical steps that include the formation of a covalent bond between the CYS481 residue of the protein and the drug molecule, as well as two protonation and deprotonation reactions.
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