Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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

Biochim Biophys Acta

Publication Date

10/2015

Volume

1854

Pages

1595 - 1604

Keywords

Cancer cell panel profiling, Conformational selection, DFG in–out transition, Kinase inhibition profile, Kinase inhibitor, Amino Acid Sequence, Binding Sites, Computational Biology, Humans, Protein Binding, Protein Conformation, Protein Kinase Inhibitors, Protein Kinases, Proto-Oncogene Proteins c-abl, src-Family Kinases