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Conformation-Selective Analogues of Dasatinib Reveal Insight into Kinase Inhibitor Binding and Selectivity
Author(s) -
Frank E. Kwarcinski,
Kristoffer Brandvold,
Sameer Phadke,
Omar M. Beleh,
Taylor K. Johnson,
Jennifer L. Meagher,
Markus A. Seeliger,
Jeanne A. Stuckey,
Matthew B. Soellner
Publication year - 2016
Publication title -
acs chemical biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.899
H-Index - 111
eISSN - 1554-8937
pISSN - 1554-8929
DOI - 10.1021/acschembio.5b01018
Subject(s) - kinome , dasatinib , chemistry , stereochemistry , selectivity , kinase , binding site , enzyme inhibitor , biochemistry , protein kinase a , enzyme , combinatorial chemistry , signal transduction , tyrosine kinase , catalysis
In the kinase field, there are many widely held tenets about conformation-selective inhibitors that have yet to be validated using controlled experiments. We have designed, synthesized, and characterized a series of kinase inhibitor analogues of dasatinib, an FDA-approved kinase inhibitor that binds the active conformation. This inhibitor series includes two Type II inhibitors that bind the DFG-out inactive conformation and two inhibitors that bind the αC-helix-out inactive conformation. Using this series of compounds, we analyze the impact that conformation-selective inhibitors have on target binding and kinome-wide selectivity.

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