Related Experiment Video
Updated: Jul 20, 2026
Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
Published on: May 17, 2024
Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by
Angeles Canales-Mayordomo1, Rosa Fayos, Jesús Angulo
1Departamento de Estructura y Función de Proteínas, Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu, 9, 28006, Madrid, Spain.
Abstract:
The binding site and backbone dynamics of a bioactive complex formed by the acidic fibroblast growth factor (FGF-1) and a specifically designed heparin hexasaccharide has been investigated by HSQC and relaxation NMR methods. The comparison of the relaxation data for the free and bound states has allowed showing that the complex is monomeric, and still induces mutagenesis, and that the protein backbone presents reduced motion in different timescale in its bound state, except in certain points that are involved in the interaction with the fibroblast growth factor receptor (FGFR).
