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Related Experiment Videos

Structure of complement component C2A: implications for convertase formation and substrate binding.

Fin J Milder1, Hans C A Raaijmakers, Mitja D A A Vandeputte

  • 1Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Faculty of Science, Utrecht University, 3584 CH Utrecht, The Netherlands.

Structure (London, England : 1993)
|October 10, 2006
PubMed
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Complement C2a

Area of Science:

  • Structural biology
  • Immunology
  • Complement system

Background:

  • C2a is essential for complement convertase activity in classical and lectin pathways.
  • Understanding C2a structure is key to deciphering complement activation.

Purpose of the Study:

  • To elucidate the structural basis of C2a function.
  • To investigate the activation mechanisms of C2a and its interaction with ligands.

Main Methods:

  • X-ray crystallography of full-length C2a.
  • Structural analysis of C2a with and without a pseudo ligand.

Main Results:

  • C2a structures reveal near-active serine protease catalytic center.
  • Von Willebrand factor A-type domains show an intermediate activation state with an open metal-ion-dependent adhesion site.

Related Experiment Videos

  • N-terminal residues are buried, suggesting a C2 to C2a structural switch.
  • Protease domain loops may interact with substrate C3.

    • Conclusions:

    • Open adhesion site enhances C4b binding, akin to integrin signaling.
    • Structural features suggest mechanisms for high substrate specificity in convertases.
    • The findings provide insights into complement pathway regulation.