Figure 7

Interactions between primary anchor residues at the N- and C-termini of the peptides and the cleft of HLA-A*11:01. (a) Interactions of P2-Ser of SSCSSCPLSK (green) with HLA-A*11:01. (b) Interactions of P10-Lys of SSCSSCPLSK (green) with HLA-A*11:01. (c) Interactions between N-terminal residue P4-Ser of SSCPLSK (orange) and heavy chain (d) Interactions between P10-Lys of SSCPLSK (orange) and HLA-A*11:01 heavy chain. (e) Interactions of primary anchor residue P2-Ser of SSCSSC (from SSCSSC + SSCPLSK) (dark blue) when bound to HLA-A*11:01. (f) P10-Lys of SSCPLSK (from SSCSSC + SSCPLSK) (magenta) when bound to HLA-A*11:01. Peptide residues are shown in sticks following the same colour scheme. The interacting residues of HLA-A*11:01 molecule are shown in cyan sticks. The direct hydrogen bonding and salt bridges between peptide residues and HLA molecule are shown as black dashed lines. The selected water molecules are shown as red spheres and the interactions mediated via water molecules are shown as red dashed lines. (g) Summary diagram indicating the canonical and non-canonical modes of peptide occupancy in MHC-I for antigen presentation.