Dipeptides promote folding and peptide binding of MHC class I molecules
Dipeptides promote folding and peptide binding of MHC class I molecules
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DOI:
10.1073/pnas.1308672110
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发表时间:
2013-09
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影响因子:
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通讯作者:
S. Saini;Katja Ostermeir;V. Ramnarayan;H. Schuster;M. Zacharias;S. Springer
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作者:
S. Saini;Katja Ostermeir;V. Ramnarayan;H. Schuster;M. Zacharias;S. Springer
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 high-affinity peptide.