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Related Experiment Videos

An atomic resolution structure for human fibroblast growth factor 1.

Matthew J Bernett1, Thayumanasamy Somasundaram, Michael Blaber

  • 1Institute of Molecular Biophysics and Department of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida 32306-4380, USA.

Proteins
|September 24, 2004
PubMed
Summary

High-resolution X-ray crystallography reveals structural insights into human fibroblast growth factor 1 (FGF-1). The study identifies core-packing defects and domain motions linked to FGF-1

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Area of Science:

  • Structural Biology
  • Protein Crystallography
  • Biochemistry

Background:

  • Fibroblast growth factor 1 (FGF-1) is a key signaling protein belonging to the beta-trefoil superfold family.
  • The beta-trefoil superfold is characterized by its unique 3-fold structural symmetry.
  • Understanding FGF-1's structure is crucial for elucidating its biological functions and interactions.

Purpose of the Study:

  • To determine the atomic resolution X-ray structure of human FGF-1.
  • To investigate the relationship between structural features, thermal stability, and ligand-binding functionalities.
  • To analyze domain motions within FGF-1 using refined atomic displacement parameters.

Main Methods:

  • Atomic resolution (1.10-Å) X-ray structure determination of human FGF-1.

Related Experiment Videos

  • High-quality diffraction data enabling unambiguous assignment of rotamers and refinement of anisotropic displacement parameters (ADPs).
  • Translation/libration/screw (TLS) analysis of putative rigid body domains.

    • Main Results:

    • The FGF-1 structure reveals numerous core-packing defects, potentially affecting thermal stability and permitting domain motions.
    • TLS analysis identifies beta-strands 6-12 as a rigid body, distinct from the more flexible beta-strands 1-5.
    • Heparin-binding sites are localized to beta-strands 6-12, while receptor-binding sites are primarily in beta-strands 1-5.

    Conclusions:

    • The identified structural defects and domain motions in FGF-1 are intrinsically linked to its heparin and receptor binding capabilities.
    • The distinct mobilities of different beta-strand regions correlate with their specific ligand-binding roles.
    • This high-resolution structural data provides a foundation for understanding FGF-1's mechanism of action.