Crystal structures of two H-2Db/glycopeptide complexes suggest a molecular basis for CTL cross-reactivity.

Glithero, A; Tormo, J; Haurum, JS; Arsequell, G; Valencia, G; Edwards, J; Springer, S; Townsend, A; Pao, YL; Wormald, M; Dwek, RA; Jones, EY; Elliott, T

Abstract:

Two synthetic O-GlcNAc-bearing peptides that elicit H-2Db-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-2Db glycopeptide complexes to 2.85 A 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 respect...

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APA Style

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. (1999). Crystal structures of two H-2Db/glycopeptide complexes suggest a molecular basis for CTL cross-reactivity. Immunity, 10(1), 63–74.

MLA Style

Glithero, A., et al. “Crystal Structures of Two H-2Db/Glycopeptide Complexes Suggest a Molecular Basis for CTL Cross-Reactivity.” Immunity, vol. 10, no. 1, 1999, pp. 63–74.

Chicago Style

Glithero, A, J Tormo, JS Haurum, G Arsequell, G Valencia, J Edwards, S Springer, et al. 1999. “Crystal Structures of Two H-2Db/Glycopeptide Complexes Suggest a Molecular Basis for CTL Cross-Reactivity.” Immunity 10 (1): 63–74.
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