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Related Experiment Videos

Structure of human factor D. A complement system protein at 2.0 A resolution

S V Narayana1, M Carson, O el-Kabbani

  • 1Center for Macromolecular Crystallography, University of Alabama at Birmingham 35294.

Journal of Molecular Biology
|January 14, 1994
PubMed
Summary

The first 3D structure of complement Factor D, a serine protease, reveals unique active site conformations. This finding offers insights into the alternative complement pathway

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Immunology

Background:

  • Factor D is a critical enzyme in the alternative pathway of the complement system.
  • It belongs to the serine protease superfamily, crucial for immune responses.

Purpose of the Study:

  • To determine the three-dimensional crystal structure of complement Factor D.
  • To investigate the structural basis for its catalytic activity and substrate specificity.

Main Methods:

  • X-ray crystallography was employed to solve the enzyme's structure.
  • Multiple isomorphous replacement and molecular replacement methods were utilized.
  • The model was refined to 2.0 A resolution.

Main Results:

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  • The crystal structure revealed two distinct active site conformations in the asymmetric unit.
  • Factor D shares the general serine protease fold but possesses unique amino acid substitutions.
  • These substitutions significantly alter loops critical for catalysis and substrate specificity.

    • Conclusions:

    • This study presents the first determined three-dimensional structure of a complement serine protease, Factor D.
    • The unique structural features provide a basis for understanding its role in complement activation.
    • The findings pave the way for targeted drug design for complement-mediated diseases.