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.
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.
Canales
Angeles
A
Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu 9, 28040 Madrid, Spain, Instituto de Investigaciones Químicas, CSIC, Américo Vespucio s/n, Sevilla, Spain.
Angulo
Jesús
J
Ojeda
Rafael
R
Bruix
Marta
M
Fayos
Rosa
R
Lozano
Rosa
R
Giménez-Gallego
Guillermo
G
Martín-Lomas
Manuel
M
Nieto
Pedro M
PM
Jiménez-Barbero
Jesús
J
D000990:Antithrombin III / Q000737:chemistry / Q000378:metabolism; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D016220:Fibroblast Growth Factor 1 / Q000737:chemistry* / Q000378:metabolism; D006025:Glycosaminoglycans / Q000737:chemistry* / Q000378:metabolism; D006493:Heparin / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D009844:Oligosaccharides / Q000737:chemistry* / Q000378:metabolism
D006025:Glycosaminoglycans; D009844:Oligosaccharides; D016220:Fibroblast Growth Factor 1; D000990:Antithrombin III; D006493:Heparin