TY - JOUR
T1 - 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
AU - Canales, Angeles
AU - Angulo, Jesus
AU - Ojeda, Rafael
AU - Bruix, Marta
AU - Fayos, Rosa
AU - Lozano, Rosa
AU - Giménez-Gallego, Guillermo
AU - Martín-Lomas, Manuel
AU - Nieto, Pedro M.
AU - Jiménez-Barbero, Jesús
PY - 2005/4/27
Y1 - 2005/4/27
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=20244368809&partnerID=8YFLogxK
U2 - 10.1021/ja043363y
DO - 10.1021/ja043363y
M3 - Article
AN - SCOPUS:20244368809
SN - 0002-7863
VL - 127
SP - 5778
EP - 5779
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 16
ER -