Human major histocompatibility complex (MHC) class I molecules with disulfide traps secure disease-related antigenic peptides and exclude competitor peptides.

@article{Truscott2008HumanMH,
  title={Human major histocompatibility complex (MHC) class I molecules with disulfide traps secure disease-related antigenic peptides and exclude competitor peptides.},
  author={Steven M. Truscott and Xiaoli Wang and Lonnie P Lybarger and William E. Biddison and Cortez C McBerry and John M. Martinko and Janet M. Connolly and Gerald P. Linette and Daved H. Fremont and Ted H. Hansen and Beatriz M. Carreno},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 12},
  pages={7480-90}
}
The ongoing discovery of disease-associated epitopes detected by CD8 T cells greatly facilitates peptide-based vaccine approaches and the construction of multimeric soluble recombinant proteins (e.g. tetramers) for isolation and enumeration of antigen-specific CD8 T cells. Related to these outcomes of epitope discovery is the recent demonstration that MHC class I/peptide complexes can be expressed as single chain trimers (SCTs) with peptide, beta(2)m and heavy chain connected by linkers to form… CONTINUE READING

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