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The structure of human complement component C7 and the C5b-7 complex.

R G DiScipio1, D N Chakravarti, H J Muller-Eberhard

  • 1Department of Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037.

The Journal of Biological Chemistry
|January 5, 1988
PubMed
Summary
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Human complement component C7 is a mosaic protein with a unique molecular architecture. Its structure reveals a key role in the membrane attack complex formation and membrane anchoring.

Area of Science:

  • Molecular biology
  • Immunology
  • Structural biology

Background:

  • The human complement system is crucial for innate immunity.
  • Understanding the structure of complement components aids in deciphering immune responses.
  • Complement component C7 (C7) is a key player in the terminal pathway of complement activation.

Purpose of the Study:

  • To elucidate the molecular architecture of human complement component C7.
  • To determine the structural contributions of C7 to the membrane attack complex (MAC).

Main Methods:

  • cDNA sequencing for primary structure determination.
  • Circular dichroism for secondary structure analysis.
  • Transmission electron microscopy for tertiary and quaternary structure visualization.

Related Experiment Videos

  • Cross-linking studies to identify MAC components.

    • Main Results:

    • C7 is an 821-amino acid mosaic protein with homology to C8 and C9.
    • It possesses four cysteine-rich segments and 28 disulfide bonds.
    • Secondary structure analysis indicated significant beta-sheet and beta-turn content.
    • Electron microscopy revealed an elongated C5b-7 complex (monomers/dimers) with a leaflet and stalk.
    • The stalk, mediating membrane binding, is primarily composed of C6 and C7.

    Conclusions:

    • C7 is essential for the hydrophilic-amphiphilic transition during MAC formation.
    • C7 functions as a critical membrane anchor for the C5b-7 complex, facilitating membrane insertion.