Epitope Prediction Algorithms for Class I MHC Molecules

  • Kenneth C. Parker


When proteins are degraded in the cytoplasm of mammalian cells, some peptides are generated that have the appropriate characteristics to be transported into the endoplasmic reticulum where they can be complexed by MHC class I molecules.1 Each human or mouse cell expresses four MHC class I molecules; two at two different loci in heterozygous individuals. Additional MHC class I molecules are expressed at other loci, and may also be important in binding peptides, but are thought to be less important because they are usually expressed in lower amounts or in a smaller number of tissues. In principle, each class I molecule/peptide complex can be recognized by a specific T cell receptor on the surface of CD8+ T cells, which can thereby target the cell for destruction. Class I molecules differ from one another in between 1 and about 40 amino acids within the same species. Crystallographic analyses have demonstrated that many of these differences are directed toward the peptide-binding groove, where they help determine the specificity of peptide binding.2 Each class I molecule has a preference for peptides with a characteristic length and amino acid sequence. The exact length requirements depend on the class I molecule, but peptides that are either exactly eight or exactly nine amino acid residues long are preferentially bound for the majority of peptide sequences.


Peptide Binding Anchor Residue Epitope Prediction Algorithm Tocompatibility Complex Class Human Histocompatibility Antigen 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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© R.G. Landes Company 1996

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  • Kenneth C. Parker

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