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• W2104514755 abstract "Binding of a single-chain Fv antibody to Escherichia coli β-galactosidase (β-gal) is known to stabilize the enzyme and activate several inactive point mutants, historically called antibody-mediated enzyme formation mutants. To understand the nature of this activation, we have determined by electron cryo-microscopy the structure of the complex between β-gal and the antibody scFv13R4. Our structure localizes the scFv13R4 binding site to the crevice between domains 1 and 3 in each β-gal subunit. The mutations that scFv13R4 counteracts are located between the antibody binding site and the active site of β-gal, at one end of the TIM-barrel that forms domain 3 where the substrate lactose is hydrolyzed. The mode of binding suggests how scFv stabilizes both the active site of β-gal and the tetrameric state." @default.
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• W2104514755 date "2014-04-01" @default.
• W2104514755 modified "2023-09-26" @default.
• W2104514755 title "Molecular Mechanism of Antibody-Mediated Activation of β-galactosidase" @default.
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• W2104514755 doi "https://doi.org/10.1016/j.str.2014.01.011" @default.
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