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2006:
Canales Angeles; Lozano Rosa; López-Méndez Blanca; Angulo Jesús; Ojeda Rafael; Nieto Pedro M; Martín-Lomas Manuel; Giménez-Gallego Guillermo; Jiménez-Barbero Jesús
Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue.
The FEBS journal 2006;
273(
20):.
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.
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