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Related Experiment Videos

Heparin structure and interactions with basic fibroblast growth factor

S Faham1, R E Hileman, J R Fromm

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.

Science (New York, N.Y.)
|February 23, 1996
PubMed
Summary
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Heparin oligosaccharides bind basic fibroblast growth factor (bFGF) without altering its structure. This binding suggests heparin

Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular biology

Background:

  • Basic fibroblast growth factor (bFGF) is crucial for cell growth and development.
  • Heparin, a complex carbohydrate, is known to modulate bFGF activity.
  • Understanding their interaction is key to deciphering FGF signaling pathways.

Purpose of the Study:

  • To determine the crystal structures of bFGF complexed with heparin-derived oligosaccharides.
  • To elucidate the binding sites and structural basis of the bFGF-heparin interaction.
  • To investigate conformational changes in bFGF upon heparin binding.

Main Methods:

  • X-ray crystallography was employed to determine the high-resolution structures.
  • Complexes of bFGF with heparin tetra- and hexasaccharides were analyzed.

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  • Structural analysis focused on identifying specific amino acid residues involved in binding.

    • Main Results:

    • Crystal structures of bFGF-heparin complexes were resolved at 1.9 and 2.2 angstroms.
    • Heparin oligosaccharides bind to a conserved surface region on bFGF involving specific residues.
    • The hexasaccharide showed additional interactions with a distinct binding site.
    • No significant conformational changes were observed in bFGF upon oligosaccharide binding.

    Conclusions:

    • Heparin oligosaccharides bind to bFGF at specific sites without inducing major structural rearrangements.
    • The binding mechanism suggests heparin's role in facilitating the interaction between bFGF and its signaling partners.
    • These findings provide structural insights into the regulation of FGF signaling by heparin.