Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by N NMR relaxation methods

A. Canales-Mayordomo, R. Fayos, R. Lozano, G. Giménez-Gallego, J. Jiménez-Barbero, J. Angulo, R. Ojeda, P.M. Nieto, M. Martín-Lomas, M. Martín-Pastor

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)


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).
Original languageEnglish
Pages (from-to)225-239
Number of pages15
JournalJournal of Biomolecular NMR
Issue number4
Publication statusPublished - 1 Aug 2006

Cite this