Functional analysis of HLA-DP polymorphism: a crucial role for DPbeta residues 9, 11, 35, 55, 56, 69 and 84-87 in T cell allorecognition and peptide binding.

@article{Daz2003FunctionalAO,
  title={Functional analysis of HLA-DP polymorphism: a crucial role for DPbeta residues 9, 11, 35, 55, 56, 69 and 84-87 in T cell allorecognition and peptide binding.},
  author={Gema D{\'i}az and M Amicosante and Dolores Jaraquemada and Richard H. Butler and M Victoria Guill{\'e}n and Miguel A. Sanchez and C{\'e}sar Nombela and Javier Arroyo},
  journal={International immunology},
  year={2003},
  volume={15 5},
  pages={565-76}
}
The information available on the specific function of HLA-DP and the structure-function relationships is very limited. Here, single amino acid substitutions of HLA-DPB1*02012 have been used to analyze the role of polymorphic residues of the DPbeta1 domain on DP-mediated T cell allorecognition and peptide binding. Using a panel of specific anti-HLA-DP mAb, we identified the HLA-DP residues involved in the recognition by these mAb, with a crucial role for DPbeta56 for most of the mAb assayed… CONTINUE READING