Abstract
The crystal structure of an efficient Diels-Alder antibody catalyst at 1.9 angstrom resolution reveals almost perfect shape complementarity with its transition state analog. Comparison with highly related progesterone and Diels-Alderase antibodies that arose from the same primordial germ line template shows the relatively subtle mutational steps that were able to evolve both structural complementarity and catalytic efficiency.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Antibodies, Catalytic / chemistry*
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Antibodies, Catalytic / genetics
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Antibodies, Catalytic / metabolism*
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Binding Sites, Antibody
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Catalysis
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Chemical Phenomena
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Chemistry, Physical
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Crystallography, X-Ray
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Evolution, Molecular*
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Haptens / chemistry
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Haptens / metabolism
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Hydrogen Bonding
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Immunoglobulin Fab Fragments / chemistry
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Immunoglobulin Fab Fragments / metabolism
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Ligands
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Models, Molecular
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Mutation
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Progesterone / immunology
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Protein Conformation
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Solubility
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Temperature
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Templates, Genetic
Substances
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Antibodies, Catalytic
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Haptens
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Immunoglobulin Fab Fragments
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Ligands
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Progesterone