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

J Am Chem Soc. 2005 Apr 27;127(16):5778-9. doi: 10.1021/ja043363y.

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 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antithrombin III / chemistry
  • Antithrombin III / metabolism
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Fibroblast Growth Factor 1 / chemistry*
  • Fibroblast Growth Factor 1 / metabolism
  • Glycosaminoglycans / chemistry*
  • Glycosaminoglycans / metabolism
  • Heparin / chemistry*
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular / methods
  • Oligosaccharides / chemistry*
  • Oligosaccharides / metabolism

Substances

  • Glycosaminoglycans
  • Oligosaccharides
  • Fibroblast Growth Factor 1
  • Antithrombin III
  • Heparin