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Chemistry. 2018 Jun 4;24(31):7861-7865. doi: 10.1002/chem.201801770. Epub 2018 May 3.

Structural Characterization of the Interaction of the Fibroblast Growth Factor Receptor with a Small Molecule Allosteric Inhibitor.

Author information

1
Goethe University, Center for Biomolecular Magnetic Resonance (BMRZ), Institute for Organic Chemistry and Chemical Biology, Max von Laue-Straße 7, 60438, Frankfurt am Main, Germany.
2
Goethe University, Center for Biomolecular Magnetic Resonance (BMRZ), Institute for Biophysical Chemistry, Max von Laue-Straße 9, 60438, Frankfurt am Main, Germany.
3
Goethe University, Institute of Pharmaceutical Chemistry, Max von Laue-Straße 9, 60438, Frankfurt, Germany.
4
German Cancer Research Center (DKFZ), Partner facility Frankfurt/Mainz.

Abstract

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), 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.

KEYWORDS:

FGFR; NMR Spectroscopy; SSR128129E; allostery; inhibitor

PMID:
29656465
DOI:
10.1002/chem.201801770
[Indexed for MEDLINE]

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