Dipeptides promote folding and peptide binding of MHC class i molecules

Sunil Kumar Saini, Katja Ostermeir, Venkat Raman Ramnarayan, Heiko Schuster, Martin Zacharias, Sebastian Springer

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

MHC class I molecules bind only those peptides with high affinity that conform to stringent length and sequence requirements. We have now investigated which peptides can aid the in vitro folding of class I molecules, and we find that the dipeptide glycyl-leucine efficiently supports the folding of HLA-A*02:01 and H-2Kb into a peptide-receptive conformation that rapidly binds high-affinity peptides. Treatment of cells with glycyl-leucine induces accumulation of peptide-receptive H-2Kb and HLA-A*02:01 at the surface of cells. Other dipeptides with a hydrophobic second amino acid show similar enhancement effects. Our data suggest that the dipeptides bind into the F pocket like the C-terminal amino acids of a highaffinity peptide. antigen presentation | ligand exchange | chemical chaperones | endoplasmic reticulum | quality control.

Original languageEnglish
Pages (from-to)15383-15388
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume110
Issue number38
DOIs
StatePublished - 17 Oct 2013
Externally publishedYes

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