Conformational Flexibility of a Synthetic Glycosylaminoglycan Bound to a Fibroblast Growth Factor. FGF-1 Recognizes Both the 1C4 and 2So Conformations of a Bioactive Heparin-like Hexasaccharide.

The article examines the conformational flexibility of a synthetic glycosylaminoglycan (GAGs) bound to a fibroblast growth factor (FGF). The study of the molecular recognition of carbohydrates by protein receptors at atomic level has attracted considerable interest during the past few years, due to their key role in a variety of relevant physiological processes. In particular, major attention has been paid to the study of the biological, structural, and conformational details of the binding of GAGs to polypeptides of the FGF family.