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

Canales-Mayordomo, A., Fayos, R., Lozano, R., Giménez-Gallego, G., Jiménez-Barbero, J., Angulo, J., Ojeda, R., Nieto, P.M., Martín-Lomas, M. and Martín-Pastor, M. (2006) Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by N NMR relaxation methods. Journal of Biomolecular NMR, 35 (4). pp. 225-239. ISSN 0925-2738

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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).

Item Type: Article
Faculty \ School: Faculty of Science > School of Pharmacy
Related URLs:
Depositing User: Pure Connector
Date Deposited: 21 Oct 2013 20:10
Last Modified: 21 Apr 2020 22:01
URI: https://ueaeprints.uea.ac.uk/id/eprint/43755
DOI: 10.1007/s10858-006-9024-y

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