Revolves around the protein structure of catalytic kinase domains and the way kinase inhibitors can interact with them. Based on the underlying systematic and consistent protocol all (currently human and mouse) kinase structures and the binding mode of kinase ligands can be directly compared to each other. Moreover, because of the classification of an all-encompassing binding site of 85 residues it is possible to compare the interaction patterns of kinase-inhibitors to each other to, for example, identify crucial interactions determining kinase-inhibitor selectivity.
Division of Medicinal Chemistry, Amsterdam Institute for Molecules, Medicines and Systems (AIMMS), Vrije Universiteit Amsterdam, Amsterdam, Netherlands
KLIFS funding source(s)
Amsterdam Academic Alliance (AAA Data Science project: Integration of Phenotypic Drug Efficacy and Molecular Chemogenomics Data) and the Netherlands eScience Center (NLeSC)/Netherlands Organisation for Scientific Research (NWO) (Enabling Technologies project: 3D-e-Chem) [027.014.201]