Crystal Structures of Two H-2D super(b)/Glycopeptide Complexes Suggest a Molecular Basis for CTL Cross-Reactivity

Two synthetic O-GlcNAc-bearing peptides that elicit H-2D super(b)-restricted glycopeptide-specific cytotoxic T cells (CTL) have been shown to display nonreciprocal patterns of cross-reactivity. Here, we present the crystal structures of the H-2D super(b) glycopeptide complexes to 2.85 Angstrom resol...

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Published in:Immunity (Cambridge, Mass.) Mass.), 1999-01, Vol.10 (1), p.63-74
Main Authors: Glithero, A, Tormo, J, Haurum, J S, Arsequell, G, Valencia, G, Edwards, J, Springer, S, Townsend, A, Pao, Y-L, Wormald, M, Dwek, R A, Jones, E Y, Elliott, T
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Language:English
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Summary:Two synthetic O-GlcNAc-bearing peptides that elicit H-2D super(b)-restricted glycopeptide-specific cytotoxic T cells (CTL) have been shown to display nonreciprocal patterns of cross-reactivity. Here, we present the crystal structures of the H-2D super(b) glycopeptide complexes to 2.85 Angstrom resolution or better. In both cases, the glycan is solvent exposed and available for direct recognition by the T cell receptor (TCR). We have modeled the complex formed between the MHC-glycopeptide complexes and their respective TCRs, showing that a single saccharide residue can be accommodated in the standard TCR-MHC geometry. The models also reveal a possible molecular basis for the observed cross-reactivity patterns of the CTL clones, which appear to be influenced by the length of the CDR3 loop and the nature of the immunizing ligand.
ISSN:1074-7613