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Related Experiment Videos

Three-dimensional structure of an antibody-antigen complex.

S Sheriff1, E W Silverton, E A Padlan

  • 1Laboratory of Molecular Biology, National Institute of Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20892.

Proceedings of the National Academy of Sciences of the United States of America
|November 1, 1987
PubMed
Summary

This study reveals the 3D structure of an antilysozyme antibody fragment (Fab)-lysozyme complex. Key interactions involve charged amino acids and specific regions on both proteins, providing insights into antibody-antigen binding.

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Area of Science:

  • Structural Biology
  • Immunology
  • Protein Crystallography

Background:

  • Antibody-antigen interactions are crucial for immune responses.
  • Understanding the structural basis of these interactions informs therapeutic development.

Purpose of the Study:

  • To determine the three-dimensional structure of an antilysozyme Fab-lysozyme complex.
  • To elucidate the molecular details of the antibody-antigen interface.

Main Methods:

  • X-ray crystallography was employed to analyze two crystal forms of the complex.
  • Detailed structural analysis of the protein-protein interface was performed.

Main Results:

  • The epitope on lysozyme spans three distinct subsites, with a major site from Gln-41 to Tyr-53.

Related Experiment Videos

  • Specific arginine residues on lysozyme interact with negatively charged residues on the antibody's heavy chain.
  • The interface surface area is approximately 26 x 19 Å, with no intervening water molecules.

    • Conclusions:

    • The antilysozyme antibody recognizes a discontinuous epitope on lysozyme.
    • The binding involves complementary charged residues and specific structural features, including a groove-ridge interaction.
    • Lysozyme's backbone remains largely unperturbed, with minor local adjustments at the epitope.