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© 2015 Elsevier B.V. All rights reserved. Recent advances in understanding the activity and selectivity of kinase inhibitors and their relationships to protein structure are presented. Conformational selection in kinases is studied from empirical, data-driven and simulation approaches. Ligand binding and its affinity are, in many cases, determined by the predetermined active and inactive conformation of kinases. Binding affinity and selectivity predictions highlight the current state of the art and advances in computational chemistry as it applies to kinase inhibitor discovery. Kinome wide inhibitor profiling and cell panel profiling lead to a better understanding of selectivity and allow for target validation and patient tailoring hypotheses. This article is part of a Special Issue entitled: Inhibitors of Protein Kinases.

Original publication

DOI

10.1016/j.bbapap.2015.03.014

Type

Journal article

Journal

Biochimica et Biophysica Acta - Proteins and Proteomics

Publication Date

01/10/2015

Volume

1854

Pages

1595 - 1604