Related Experiment Video
Updated: Feb 11, 2026

Synthesis of Masarimycin, a Small Molecule Inhibitor of Gram-Positive Bacterial Growth
Published on: January 7, 2022
Structural Characterization of the Interaction of the Fibroblast Growth Factor Receptor with a Small Molecule
Franziska Kappert1, Sridhar Sreeramulu1, Hendrik R A Jonker1
1Goethe University, Center for Biomolecular Magnetic Resonance (BMRZ), Institute for Organic Chemistry and Chemical Biology, Max von Laue-Straße 7, 60438, Frankfurt am Main, Germany.
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.
More Related Videos
07:32Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library
Published on: September 30, 2019
10:17Methodologies for Studying B. subtilis Biofilms as a Model for Characterizing Small Molecule Biofilm Inhibitors
Published on: October 9, 2016
Related Concept Videos
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
Eukaryotic Transcription Inhibitors
Eukaryotic transcription inhibitors usually contain two distinct domains, a...
Drug-Receptor Interactions
Several parameters, such as the drug's affinity for its receptor and its efficacy, which is its ability to activate the receptor, determine the drug's effect on the tissue....
Role of Hematopoietic Growth Factors
Thrombopoietin (TPO), mainly released by the liver,...
Factors Influencing Microbial Growth: pH