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. ORCID: https://orcid.org/0000-0001-7250-5639, 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

Full text not available from this repository.

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 (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Drug Delivery and Pharmaceutical Materials (former - to 2017) Faculty of Science > Research Groups > Pharmaceutical Materials and Soft Matter
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	Pure Connector
Date Deposited:	21 Oct 2013 20:10
Last Modified:	24 Sep 2024 10:42
URI:	https://ueaeprints.uea.ac.uk/id/eprint/43755
DOI:	10.1007/s10858-006-9024-y

Actions (login required)

View Item