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Canales, Angeles, Lozano, Rosa, López-Méndez, Blanca, Angulo, Jesús 
ORCID: https://orcid.org/0000-0001-7250-5639, Ojeda, Rafael, Nieto, Pedro M., Martín-Lomas, Manuel, Giménez-Gallego, Guillermo and Jiménez-Barbero, Jesús
(2006)
Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue.
FEBS Journal, 273 (20).
pp. 4716-4727.
ISSN 1742-464X
Abstract
The 3D structure of a complex formed by the acidic fibroblast growth factor (FGF-1) and a specifically designed synthetic heparin hexasaccharide has been determined by NMR spectroscopy. This hexasaccharide can substitute natural heparins in FGF-1 mitogenesis assays, in spite of not inducing any apparent dimerization of the growth factor. The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments. Our results confirm that glycosaminoglycans induced FGF-1 dimerization either in a cis or trans disposition with respect to the heparin chain is not an absolute requirement for biological activity.
| Item Type: | Article |
|---|---|
| Faculty \ School: | Faculty of Science > School of Pharmacy (former - to 2024) |
| UEA Research Groups: | Faculty of Science > Research Groups > Pharmaceutical Materials and Soft Matter Faculty of Science > Research Groups > Drug Delivery and Pharmaceutical Materials (former - to 2017) |
| Related URLs: | |
| Depositing User: | Pure Connector |
| Date Deposited: | 21 Oct 2013 20:00 |
| Last Modified: | 24 Sep 2024 10:42 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/43757 |
| DOI: | 10.1111/j.1742-4658.2006.05474.x |
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