Conformational flexibility of a synthetic glycosylaminoglycan bound to a fibroblast growth factor. FGF-1 recognizes both the C and S conformations of a bioactive heparin-like hexasaccharide

Canales, Angeles, Angulo, Jesus, Ojeda, Rafael, Bruix, Marta, Fayos, Rosa, Lozano, Rosa, Giménez-Gallego, Guillermo, Martín-Lomas, Manuel, Nieto, Pedro M. and Jiménez-Barbero, Jesús (2005) Conformational flexibility of a synthetic glycosylaminoglycan bound to a fibroblast growth factor. FGF-1 recognizes both the C and S conformations of a bioactive heparin-like hexasaccharide. Journal of the American Chemical Society, 127 (16). pp. 5778-5779. ISSN 0002-7863

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Abstract

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 C-labeled protein and a regular C 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.

Item Type: Article
Faculty \ School: Faculty of Science > School of Pharmacy
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Depositing User: Pure Connector
Date Deposited: 21 Oct 2013 20:08
Last Modified: 17 Mar 2020 18:44
URI: https://ueaeprints.uea.ac.uk/id/eprint/43756
DOI: 10.1021/ja043363y

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