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

Research output: Contribution to journalArticlepeer-review

20 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

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Distortion of the major histocompatibility complex class i binding groove to accommodate an insulin-derived 10-mer peptide'. Together they form a unique fingerprint.

Cite this