Crystal structure of a non-canonical low-affinity peptide complexed with MHC class I: a new approach for vaccine design.

@article{Apostolopoulos2002CrystalSO,
  title={Crystal structure of a non-canonical low-affinity peptide complexed with MHC class I: a new approach for vaccine design.},
  author={Vasso Apostolopoulos and Minmin Yu and Adam L. Corper and Luc Teyton and Geoffrey A. Pietersz and Ian F.C. Mckenzie and Ian A. Wilson and Magdalena Plebanski},
  journal={Journal of molecular biology},
  year={2002},
  volume={318 5},
  pages={1293-305}
}
Peptides bind with high affinity to MHC class I molecules by anchoring certain side-chains (anchors) into specificity pockets in the MHC peptide-binding groove. Peptides that do not contain these canonical anchor residues normally have low affinity, resulting in impaired pMHC stability and loss of immunogenicity. Here, we report the crystal structure at 1.6 A resolution of an immunogenic, low-affinity peptide from the tumor-associated antigen MUC1, bound to H-2Kb. Stable binding is still… CONTINUE READING
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