Crystal structure of the complex between human CD8alpha(alpha) and HLA-A2.

@article{Gao1997CrystalSO,
  title={Crystal structure of the complex between human CD8alpha(alpha) and HLA-A2.},
  author={George F. Gao and Jos{\'e} Tormo and Ulrich C. Gerth and Jessica R. Wyer and Andrew J McMichael and David I Stuart and John I. Bell and Edith Yvonne Jones and Bent K. Jakobsen},
  journal={Nature},
  year={1997},
  volume={387 6633},
  pages={630-4}
}
The dimeric cell-surface glycoprotein CD8 is crucial to the positive selection of cytotoxic T cells in the thymus. The homodimer CD8alpha(alpha) or the heterodimer alpha beta stabilizes the interaction of the T-cell antigen receptor (TCR) with major histocompatibility complex (MHC) class I/peptide by binding to the class I molecule. Here we report the crystal structure at 2.7 A resolution of a complex between CD8alpha(alpha) and the human MHC molecule HLA-A2, which is associated with peptide… CONTINUE READING