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Published on: May 6, 2011
Three-dimensional structures of acidic and basic fibroblast growth factors
1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.
Science (New York, N.Y.)
|January 4, 1991
Summary
Structural analysis of fibroblast growth factor (FGF) reveals a conserved protein fold. This structure provides insights into receptor and heparin binding sites, crucial for cell proliferation and differentiation.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Fibroblast growth factors (FGFs) are key regulators of cell proliferation and differentiation.
- Receptor-mediated pathways are essential for FGF signaling.
- Understanding FGF structure is critical for elucidating its biological functions.
Purpose of the Study:
- To determine the three-dimensional structures of bovine acidic FGF and human basic FGF.
- To identify conserved structural features and potential functional sites within the FGF family.
- To compare FGF structure with other related proteins.
Main Methods:
- Crystallographic determination of protein structures.
- Analysis of protein folding patterns and internal symmetry.
- Sequence analysis to identify conserved regions and functional sites.
Main Results:
- The three-dimensional structures of bovine acidic FGF and human basic FGF were determined.
- Both structures exhibit a conserved fold of 12 antiparallel beta strands with approximate threefold internal symmetry.
- Identified potential receptor and heparin binding sites, including beta-sheet strand 10.
- Observed topological similarity to soybean trypsin inhibitor and interleukins-1 beta and -1 alpha.
Conclusions:
- The conserved FGF protein fold is fundamental to its function.
- Specific structural regions are implicated in receptor and heparin binding.
- Structural similarities suggest evolutionary relationships and shared functional mechanisms with other protein families.
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