Abstract
Ten years have passed since the initial reports that antibodies could be programmed to have enzymatic activity by immunization with a transition-site analog. Much of the research over the last decade has focused on defining the scope and generality of antibody catalysis; however, during the past two years the first few crystal structures of catalytic antibody transition- state analogs have been reported. This review analyzes four such structures of catalytic antibodies that catalyze markedly different reactions, including ester hydrolysis, sulfide oxidation, and a pericyclic rearrangement. Structure-function relations for these catalysts are discussed and compared to the structure and function of natural enzymes, as well as the chemistry that occurs in solution.
Original language | English (US) |
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Pages (from-to) | 461-493 |
Number of pages | 33 |
Journal | Annual Review of Biophysics and Biomolecular Structure |
Volume | 26 |
DOIs | |
State | Published - 1997 |
Externally published | Yes |
Keywords
- Abzymes
- Antigen binding
- Catalysis
- Catalytic mechanism
ASJC Scopus subject areas
- Biophysics
- Structural Biology