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Crystal structure of basic fibroblast growth factor at 1.6 A resolution.
H Ago1, Y Kitagawa, A Fujishima
1Institute for Protein Research, Osaka University.
Journal of Biochemistry
|September 1, 1991
Summary
Crystal structures of human basic fibroblast growth factor (hFGF) were determined. The serine analogue and wild-type forms showed nearly identical structures, revealing a potential heparin-binding site.
Area of Science:
- Structural biology
- Protein crystallography
Background:
- Human basic fibroblast growth factor (hFGF) plays crucial roles in cell growth and differentiation.
- Understanding its three-dimensional structure is essential for elucidating its function and interactions.
Purpose of the Study:
- To determine the high-resolution crystal structures of wild-type hFGF and its serine analogue.
- To identify structural features, including potential ligand-binding sites.
Main Methods:
- X-ray crystallography was employed to determine the structures.
- Multiple isomorphous replacement phasing was used.
- Structure refinement was performed using stereochemically restrained methods.
Main Results:
- Crystal structures were obtained at 1.6 Å (serine analogue) and 2.5 Å (wild-type) resolution.
- The structures of the serine analogue and wild-type hFGF were nearly identical (RMSD of 0.11 Å for Cα atoms).
- A potential heparin-binding site involving five basic residues was identified through electrostatic potential calculations.
Conclusions:
- The determined structures provide detailed insights into the architecture of hFGF.
- The identified heparin-binding site suggests a mechanism for hFGF-heparin interaction.
- The structural similarity highlights the stability of the hFGF fold.