Implication of HLA-DR residues at positions 67, 71, and 86 in interaction between HLA-DR11 and peptide HA306-320.

@article{Zeliszewski1993ImplicationOH,
  title={Implication of HLA-DR residues at positions 67, 71, and 86 in interaction between HLA-DR11 and peptide HA306-320.},
  author={Dominique Zeliszewski and J J Golvano and Pierre Gaudebout and Isabelle Dorval and Catherine Freidel and Lucette Gebuhrer and Herv{\'e} Betuel and F Borr{\'a}s-Cuesta and Ghislaine Sterkers},
  journal={Journal of immunology},
  year={1993},
  volume={151 11},
  pages={6237-47}
}
To get further insight into the role of three polymorphic DR residues located in one alpha-helix of the HLA-DR binding groove, we studied how natural substitutions at positions 67, 71, and 86 on DR11 molecules influence MHC binding and/or T cell recognition of peptide HA306-320 and of monosubstituted peptide analogues. Our results show that: 1) Reactivities of all HA306-320-specific T cell clones tested are decreased by DR substitution at position 86 and can even be lowered by additional… CONTINUE READING