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• W2083663804 endingPage "1933" @default.
• W2083663804 startingPage "1929" @default.
• W2083663804 abstract "The three-dimensional structure of an antibody (39-A11) that catalyzes a Diels-Alder reaction has been determined. The structure suggests that the antibody catalyzes this pericyclic reaction through a combination of packing and hydrogen-bonding interactions that control the relative geometries of the bound substrates and electronic distribution in the dienophile. A single somatic mutation, serine-91 of the light chain to valine, is largely responsible for the increase in affinity and catalytic activity of the affinity-matured antibody. Structural and functional studies of the germ-line precursor suggest that 39-A11 and related antibodies derive from a family of germ-line genes that have been selected throughout evolution for the ability of the encoded proteins to form a polyspecific combining site. Germ line–encoded antibodies of this type, which can rapidly evolve into high-affinity receptors for a broad range of structures, may help to expand the binding potential associated with the structural diversity of the primary antibody repertoire." @default.
• W2083663804 created "2016-06-24" @default.
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• W2083663804 date "1998-03-20" @default.
• W2083663804 modified "2023-10-10" @default.
• W2083663804 title "Immunological Origins of Binding and Catalysis in a Diels-Alderase Antibody" @default.
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• W2083663804 doi "https://doi.org/10.1126/science.279.5358.1929" @default.
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