Fig. 4: Models of peptide/MHC I complexes indicate structural and physical correlates with immunogenicity.
From: Reversion analysis reveals the in vivo immunogenicity of a poorly MHC I-binding cancer neoepitope
a For the tumor rejecting TYIRPFETKVK neoepitope, the leucine-to-phenylalanine substitution at position 6 is predicted to increase hydrophobic solvent accessibility by 17 Å2, with the aromatic phenylalanine ring partially exposed for interactions with T cell receptors. An overlay of the neoepitope and its wild type counterpart demonstrates the substantial differences between the wild type peptide and neoepitope. b For the tumor rejecting YIRPFETKVK neoepitope, with the leucine-to-phenylalanine substitution now at position 5, the modeling predicts structural alterations in exposed side chains in response to the mutation, as well as a reduction in exposed hydrophobic solvent accessible surface area of 23 Å2.
