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Related Experiment Videos

Complement regulation at the molecular level: the structure of decay-accelerating factor.

P Lukacik1, P Roversi, J White

  • 1Laboratory of Molecular Biophysics and Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, England.

Proceedings of the National Academy of Sciences of the United States of America
|January 22, 2004
PubMed
Summary

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The complement regulator CD55, crucial for protecting cells, adopts a rod-like structure. Its function relies on a specific hydrophobic patch interacting with the convertase for effective complement regulation.

Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • CD55 is a vital human complement regulator, preventing self-cell damage.
  • It protects cells from complement-mediated lysis, a critical immune process.

Purpose of the Study:

  • To elucidate the structural arrangement and membrane-proximal organization of CD55.
  • To identify the molecular mechanisms underlying CD55's interaction with the convertase for complement regulation.

Main Methods:

  • X-ray diffraction and analytical ultracentrifugation were used to determine CD55 structure in crystal and solution.
  • Mutation mapping and hydrophobic potential analysis were employed to investigate functional interactions.

Main Results:

Related Experiment Videos

  • CD55 exhibits a rod-like structure comprising four short consensus repeat (SCR) domains.
  • An extended stalk with 11 O-glycans positions the SCR domains approximately 177 Å above the cell membrane.
  • A hydrophobic patch on the linker between SCR domains 2 and 3 is critical for convertase interaction and complement regulation.

    • Conclusions:

    • The structural organization of CD55, including its glycosylated stalk, is key to its positioning and function.
    • Specific hydrophobic interactions involving the SCR domain linker are essential for effective complement regulation by CD55.