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

Chihiro Motozono, James A. Pearson, Evy De Leenheer, Pierre J. Rizkallah, Konrad Beck, Andrew Trimby, Andrew K. Sewell, F. Susan Wong, David K. Cole

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17 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)18924-18933
Number of pages10
JournalJournal of Biological Chemistry
Volume290
Issue number31
DOIs
Publication statusPublished - Jul 31 2015

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All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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