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The structural and functional basis of antibody catalysis
1Department of Pharmaceutical Chemistry, University of California, San Francisco 94143, USA.
Annual Review of Biophysics and Biomolecular Structure
|January 1, 1997
Summary
Antibodies can be engineered for enzymatic activity. Recent crystal structures reveal how these catalytic antibodies function, offering insights into enzyme mechanisms and solution chemistry.
Area of Science:
- Biochemistry
- Immunology
- Structural Biology
Background:
- Antibodies have been engineered to possess enzymatic activity through immunization with transition-state analogs.
- Research has focused on the scope and generality of antibody catalysis over the past decade.
- The first crystal structures of catalytic antibody transition-state analogs have emerged in the last two years.
Purpose of the Study:
- To analyze the crystal structures of four catalytic antibodies.
- To investigate antibodies catalyzing diverse reactions: ester hydrolysis, sulfide oxidation, and pericyclic rearrangement.
- To compare the structure-function relationships of these catalytic antibodies with natural enzymes and solution chemistry.
Main Methods:
- Analysis of four reported crystal structures of catalytic antibody transition-state analogs.
- Comparative analysis of structure-function relationships.
- Comparison with natural enzyme catalysis and solution-phase chemical reactions.
Main Results:
- Detailed structural analysis of four distinct catalytic antibodies.
- Elucidation of structure-function relationships for antibody-catalyzed ester hydrolysis, sulfide oxidation, and pericyclic rearrangement.
- Comparison of catalytic antibody mechanisms to those of natural enzymes.
Conclusions:
- Catalytic antibodies exhibit diverse structures and functions.
- Structural insights provide a basis for understanding antibody catalysis.
- Comparison with natural enzymes and solution chemistry deepens our understanding of enzymatic mechanisms.