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Related Experiment Videos

Translational mini-review series on complement factor H: structural and functional correlations for factor H.

C Q Schmidt1, A P Herbert, H G Hocking

  • 1The Edinburgh Biomolecular NMR Unit, Schools of Chemistry and Biological Sciences, University of Edinburgh, Edinburgh, UK.

Clinical and Experimental Immunology
|December 18, 2007
PubMed
Summary
This summary is machine-generated.

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Complement factor H (CFH) regulates complement activation. Its structure, particularly CCP 20 and CCP 7, binds surfaces and influences disease-linked variations.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Immunology

Background:

  • Complement factor H (CFH) is a key regulator of complement system activation, abundant in human plasma.
  • CFH is a large glycoprotein composed of 20 complement control protein (CCP) modules.
  • Dysregulation of complement activation is implicated in various diseases.

Purpose of the Study:

  • To elucidate the three-dimensional structure of CFH segments and identify functional binding sites.
  • To understand the role of specific CCP modules in CFH's interaction with self-surfaces and complement components.
  • To correlate structural findings with sequence variations linked to complement-mediated disorders.

Main Methods:

  • Three-dimensional structure determination of CFH CCP module segments.

Related Experiment Videos

  • Nuclear Magnetic Resonance (NMR) spectroscopy to map glycosaminoglycan-binding sites.
  • Analysis of known sequence variations in relation to structural data.

    • Main Results:

    • Binding sites for C3b are located at the N and C termini of CFH.
    • CCP 20 and CCP 7 possess distinct glycosaminoglycan-binding patches.
    • These binding sites involve residues associated with dense deposit disease, age-related macular degeneration, and atypical hemolytic uremic syndrome.

    Conclusions:

    • CFH structure facilitates binding to self-surfaces via CCP 20 and CCP 7.
    • These interactions are crucial for distinguishing self from non-self and regulating complement activation.
    • Structural insights provide a basis for understanding the pathogenesis of associated diseases.