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Active sites in complement component C3 mapped by mutations at indels

R T Ogata1, R Ai, P J Low

  • 1Medical Biology Institute, La Jolla, CA 92037, USA. rogata@tpims.org

Journal of Immunology (Baltimore, Md. : 1950)
|October 30, 1998
PubMed
Summary
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Investigating human complement component C3, researchers engineered mutants to identify protein:protein interaction sites using length polymorphisms (indels). Mutations at specific indels revealed key functional sites, aiding in understanding C3 structure and interactions.

Area of Science:

  • Immunology
  • Molecular Biology
  • Protein Science

Background:

  • The human complement component C3 is crucial for immune responses.
  • Identifying protein:protein interaction sites is vital for understanding molecular mechanisms.
  • Length polymorphisms (indels) in protein families are potential indicators of functional sites.

Purpose of the Study:

  • To test if indels in complement component C3 can guide the identification of protein:protein interaction sites.
  • To characterize the functional impact of mutations at different indel sites within C3.
  • To elucidate the structural and functional roles of various regions within C3.

Main Methods:

  • Engineered mutants of human complement component C3 by introducing sequence changes at 27 indels.

Related Experiment Videos

  • Expressed 26 C3 mutants in transiently transfected COS cells.
  • Assayed mutant C3 proteins for concentration, hemolytic activity, proteolytic activation, and factor I susceptibility.

    • Main Results:

    • Most mutations at indels did not significantly alter C3 expression or activity.
    • Mutations at four indels severely impaired C3 functional activity without affecting protein stability or structure.
    • One indel mutation altered the equilibrium between C3 conformations, while four others reduced both activity and expression.

    Conclusions:

    • Indels located near functionally important residues are strong candidates for protein:protein interaction sites.
    • Mutational analysis of C3 indels provides insights into its structural and functional domains.
    • This approach using indels can be a valuable strategy for mapping interaction sites in other protein families.