Premium
Structural Characterization of the Interaction of the Fibroblast Growth Factor Receptor with a Small Molecule Allosteric Inhibitor
Author(s) -
Kappert Franziska,
Sreeramulu Sridhar,
Jonker Hendrik R. A.,
Richter Christian,
Rogov Vladimir V.,
Proschak Ewgenij,
Hargittay Bruno,
Saxena Krishna,
Schwalbe Harald
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201801770
Subject(s) - fibroblast growth factor receptor , allosteric regulation , fibroblast growth factor receptor 1 , fibroblast growth factor , fibroblast growth factor receptor 2 , receptor , microbiology and biotechnology , chemistry , extracellular , fibroblast growth factor receptor 3 , signal transduction , fibroblast growth factor receptor 4 , biochemistry , biology
The interaction of fibroblast growth factors (FGFs) with their fibroblast growth factor receptors (FGFRs) are important in the signaling network of cell growth and development. SSR128129E (SSR),[1][F. Bono, 2013], [2][C. Herbert, 2013] a ligand of small molecular weight with potential anti‐cancer properties, acts allosterically on the extracellular domains of FGFRs. Up to now, the structural basis of SSR binding to the D3 domain of FGFR remained elusive. This work reports the structural characterization of the interaction of SSR with one specific receptor, FGFR3, by NMR spectroscopy. This information provides a basis for rational drug design for allosteric FGFR inhibitors.