Perspective on computational and structural aspects of kinase discovery from IPK2014.

Martin E, Knapp S, Engh RA, Moebitz H, Varin T, Roux B, Meiler J, Berdini V, Baumann A, Vieth M
Biochim Biophys Acta. 2015 1854 (10 Pt B): 1595-604

PMID: 25861861 · PMCID: PMC5105597 · DOI:10.1016/j.bbapap.2015.03.014

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.

Copyright © 2015 Elsevier B.V. All rights reserved.

MeSH Terms (10)

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

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