BiomedExperts: Conformational flexibility of a synthetic glycosylaminoglycan bound to a fibroblast growth factor. FGF-1 recognizes both the (1)C(4) and (2)S(O) conformations of a bioactive heparin-like hexasaccharide.

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2005: Canales Angeles; Angulo Jesús; Ojeda Rafael; Bruix Marta; Fayos Rosa; Lozano Rosa; Giménez-Gallego Guillermo; Martín-Lomas Manuel; Nieto Pedro M; Jiménez-Barbero Jesús
Conformational flexibility of a synthetic glycosylaminoglycan bound to a fibroblast growth factor. FGF-1 recognizes both the (1)C(4) and (2)S(O) conformations of a bioactive heparin-like hexasaccharide.
Journal of the American Chemical Society 2005;127(16):5778-9.

The first direct NMR determination of the conformation of a conformationally flexible heparin-like hexasaccharide bound to a key receptor, FGF-1, is described. The determination has been based on the use of a 13C-labeled protein and a regular 12C sugar. FGF-1 recognizes several conformations of the iduronic moieties of the hexasaccharide. Therefore, this case is different than that described for the controversial recognition of heparin-like saccharides by AT-III, which seems to recognize just one conformation of the iduronic acid residues.

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