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- W1968542364 abstract "Two structurally distinct classes of peptides were recently identified by phage display that bind the high-affinity IgE receptor, FcϵRI, and block IgE binding and subsequent receptor activation. Both classes adopt highly stable structures in solution, one forming a β hairpin, with the other forming a helical “zeta” structure. Despite these differences, the two classes bind competitively to the same site on the receptor. Structural analyses of both peptide-receptor complexes by NMR spectroscopy and/or X-ray crystallography reveal that the unrelated peptide scaffolds have nevertheless converged to present a similar three-dimensional surface to interact with FcϵRI and that their modes of interaction share a key feature of the IgE-FcϵRI complex, the proline/tryptophan sandwich." @default.
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- W1968542364 date "2004-07-01" @default.
- W1968542364 modified "2023-10-16" @default.
- W1968542364 title "Convergent Recognition of the IgE Binding Site on the High-Affinity IgE Receptor" @default.
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- W1968542364 doi "https://doi.org/10.1016/j.str.2004.04.015" @default.
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