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- W2074021150 abstract "The structure of a complex of the anti-cholera toxin antibody TE33 Fab (fragment antibody) with the D-peptide vpGsqhyds was solved to 1.78 Å resolution. The D-peptide was derived from the linear L-peptide epitope VPGSQHIDS by a stepwise transformation. Despite the very similar amino acid sequence—the only difference is a tyrosine residue in position 7—there are marked differences in the individual positions with respect to their contribution to the peptide overall affinity as ascertained by a complete substitutional analysis. This is reflected by the X-ray structure of the TE33 Fab/D-peptide complex where there is an inverted orientation of the D-peptide as compared with the known structure of a corresponding complex containing the epitope L-peptide, with the side chains establishing different contacts within the binding site of TE33. The D- and L-peptide affinities are comparable and the surface areas buried by complex formation are almost the same. Thus the antibody TE33 provides a typical example for polyspecific binding behavior of IgG family antibodies. Copyright © 2007 John Wiley & Sons, Ltd." @default.
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- W2074021150 date "2007-01-01" @default.
- W2074021150 modified "2023-10-03" @default.
- W2074021150 title "Structure of an anti-cholera toxin antibody Fab in complex with an epitope-derivedD-peptide: a case of polyspecific recognition" @default.
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- W2074021150 doi "https://doi.org/10.1002/jmr.838" @default.
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