Supplementary Figure 7: In silico modeling of the APNCYGNIPL peptide conformation when bound to HLA-B*0702 | Nature Biotechnology

Supplementary Figure 7: In silico modeling of the APNCYGNIPL peptide conformation when bound to HLA-B*0702

From: T cell receptor fingerprinting enables in-depth characterization of the interactions governing recognition of peptide–MHC complexes

Supplementary Figure 7

(a) Structural model of the original peptide, APNCYGNIPL, binding to HLA-B*0702. Color scaling indicates the importance of a given amino acid for retaining the conformation of the original peptide when bound to the MHC (the information content is listed in Supplementary Data 5). (b) Bar plot of the FoldX derived ΔΔG energy between the original peptide (APNCYGNIPL) and HLA-B*0702, as well as all the peptide variants created by substituting each peptide position (x-axis) with all naturally occurring amino acids (n=19). If the ΔΔG is larger than zero it indicates that the given amino acid substitution has destabilized the peptide-MHC interaction while a ΔΔG smaller than zero indicates that the substitution has stabilized the peptide-MHC interaction. (c) Sequence logo showing the structurally predicted peptide-MHC binding preference for HLA-B*0702APN based on the energy change (ΔΔ) calculated in b.

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