NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 3 in apo state and in complex with inhibitor PD173074

Fibroblast growth factors receptors (FGFR) are transmembrane protein tyrosine kinases involved in many cellular process,

including growth, differentiation and angiogenesis. Dysregulation of FGFR enzymatic activity is associated with developmental

disorders and cancers; therefore FGFRs have become attractive targets for drug discovery, with a number of agents

in late-stage clinical trials. Here, we present the backbone resonance assignments of FGFR3 tyrosine kinase domain in the

ligand-free form and in complex with the canonical FGFR kinase inhibitor PD173074. Analysis of chemical shift changes

upon inhibitor binding highlights a characteristic pattern of allosteric network perturbations that is of relevance for future

drug discovery activities aimed at development of conformationally-selective FGFR inhibitors.