Distortion of the major histocompatibility complex class i binding groove to accommodate an insulin-derived 10-mer peptide

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Abstract

Background: CD8+ T-cells play a central role in type 1 diabetes (T1D) by recognizing insulin peptides displayed by MHC. Results: A novel flexible MHC binding mode accommodates extra C-terminal peptide residues. Conclusion: Unusual peptide-MHC binding might explain weak TCR affinity of a natural T1D epitope. Significance: MHC peptide binding can be highly flexible around the F-binding pocket.

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APA

Motozono, C., Pearson, J. A., De Leenheer, E., Rizkallah, P. J., Beck, K., Trimby, A., … Cole, D. K. (2015). Distortion of the major histocompatibility complex class i binding groove to accommodate an insulin-derived 10-mer peptide. Journal of Biological Chemistry, 290(31), 18924–18933. https://doi.org/10.1074/jbc.M114.622522

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