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Related Experiment Videos

26-10 Fab-digoxin complex: affinity and specificity due to surface complementarity

P D Jeffrey1, R K Strong, L C Sieker

  • 1Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ 08543-4000.

Proceedings of the National Academy of Sciences of the United States of America
|November 1, 1993
PubMed
Summary
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The three-dimensional structures of an anti-digoxin antibody and its complex with digoxin reveal that specificity arises from shape complementarity, not hydrogen bonds. Digoxin binds in a deep pocket, with no significant conformational changes observed.

Area of Science:

  • Structural biology
  • Immunology
  • Biochemistry

Background:

  • Monoclonal antibodies are crucial tools in diagnostics and therapeutics.
  • Understanding antibody-antigen interactions at a molecular level is key to antibody engineering.

Purpose of the Study:

  • To determine the three-dimensional structures of the anti-digoxin monoclonal antibody 26-10.
  • To elucidate the structural basis of the high-affinity interaction between antibody 26-10 and digoxin.

Main Methods:

  • X-ray crystallography was used to determine the structures.
  • The structures were resolved at 2.7 Å (uncomplexed) and 2.5 Å (complexed with digoxin).

Main Results:

  • The antibody-antigen complex showed no significant conformational changes in either component.

Related Experiment Videos

  • Digoxin binds in a deep pocket of the antibody's combining site, primarily interacting with the heavy chain.
  • Specificity and high affinity are achieved through shape complementarity, with no hydrogen bonds or salt links formed.

    • Conclusions:

    • The 26-10-digoxin complex represents a unique antibody-antigen interaction driven by shape complementarity.
    • This finding provides insights into antibody binding mechanisms and potential for antibody design.