Figure 5: Molecular modeling of Arg substitutions in the C-terminal flanking region of the native Flu1 peptide. | Nature Communications

Figure 5: Molecular modeling of Arg substitutions in the C-terminal flanking region of the native Flu1 peptide.

From: Modification of the carboxy-terminal flanking region of a universal influenza epitope alters CD4+ T-cell repertoire selection

Figure 5

(a) HA1.7 TCR (TCRα green, TCRβ blue cartoon) bound to HLA-DR1 (grey cartoon) complexed with Flu1 (PKYVKQNTLKLAT; core region red sticks, flanking regions blue sticks). The HA1.7 TCR β-chain is beyond the limits for atomic contacts with either P10 or P11 in the native structure. (b,c) Modelling shows that a new interaction, possibly a salt bridge, could be formed between the HA1.7 TCR β-chain residue Asp28 and Arg substituted at either position 10 (b) or 11 (c) of the HA peptide. This new interaction could explain the increase in affinity observed for cognate TCR binding to Flu2 and Flu3 compared with Flu 1.

Back to article page