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Solution structure of Compstatin, a potent complement inhibitor

D Morikis1, N Assa-Munt, A Sahu

  • 1The Burnham Institute, La Jolla, California 92037, USA.

Protein Science : a Publication of the Protein Society
|April 16, 1998
PubMed
Summary
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Compstatin, a peptide inhibitor of complement component C3, has a defined structure featuring a beta-turn. Key residues like Val3, Gln5, Asp6, Trp7, and Gly8 are crucial for its potent C3 inhibition.

Area of Science:

  • Biochemistry
  • Immunology
  • Structural Biology

Background:

  • The third component of complement, C3, is central to all complement activation pathways.
  • Compstatin is a 13-residue cyclic peptide that inhibits C3 and complement activation.

Purpose of the Study:

  • To determine the solution structure of Compstatin.
  • To investigate the structure-function relationships of Compstatin's binding to C3.
  • To identify critical residues for Compstatin's inhibitory activity.

Main Methods:

  • 2D NMR spectroscopy to determine solution structure.
  • Synthesis of substitution analogues to study structure-function relationships.
  • Hybrid distance geometry-restrained simulated-annealing methodology for structure generation.

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Main Results:

  • The Compstatin structure features a type I beta-turn (Gln5-Asp6-Trp7-Gly8) and hydrophobic side-chain packing (Val3, Val4, Trp7).
  • Val3, Gln5, Asp6, Trp7, and Gly8 were identified as critical residues for inhibitory activity.
  • Substitution of Gly8 resulted in a 100-fold decrease in inhibitory potency.

Conclusions:

  • Specific side-chain interactions and the beta-turn are essential for Compstatin's conformational stability and functional activity.
  • Compstatin's structure-activity relationship provides insights into C3 inhibition.