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Three-dimensional structure of human basic fibroblast growth factor.

A E Eriksson1, L S Cousens, L H Weaver

  • 1Institute of Molecular Biology, Department of Physics, University of Oregon, Eugene.

Proceedings of the National Academy of Sciences of the United States of America
|April 15, 1991
PubMed
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The three-dimensional structure of human basic fibroblast growth factor (bFGF) was determined using X-ray crystallography. This reveals a trigonal pyramid fold, identifying potential heparin and receptor binding sites crucial for bFGF function.

Area of Science:

  • Structural Biology
  • Protein Crystallography
  • Biochemistry

Background:

  • Human basic fibroblast growth factor (bFGF) is a key signaling protein.
  • Understanding bFGF's structure is vital for elucidating its biological functions and interactions.

Purpose of the Study:

  • To determine the high-resolution three-dimensional structure of human bFGF.
  • To identify potential binding sites for heparin and its receptor.

Main Methods:

  • X-ray crystallography was employed to solve the structure of bFGF.
  • Multiple isomorphous replacement and refinement were used to achieve 2.2-A resolution.

Main Results:

  • The bFGF structure adopts a trigonal pyramid fold, similar to other growth factors.

Related Experiment Videos

  • A sulfate ion was identified at a potential heparin-binding site.
  • A distinct loop region, presumed for receptor binding, was located approximately 25 A from the heparin site.

    • Conclusions:

    • The determined structure provides insights into bFGF's molecular organization.
    • The identified binding sites offer a structural basis for understanding bFGF-heparin and bFGF-receptor interactions.
    • The structural similarity to other proteins suggests conserved functional mechanisms.