Fig. 4: Structural overview of proinsulin C-peptide-responsive TCR-HLA-DQ8-HIPL11C ternary complexes.
From: T cell receptor recognition of hybrid insulin peptides bound to HLA-DQ8
a–c Cartoon representation of TCR bound to HLA-DQ8-HIPL11C. The HLA-DQ8 α-chain is coloured in neon, and the HLA-DQ8 β-chain in light cyan. The TCRs are coloured as follows: a TCR A3.10 α-chain in sky-blue; β-chain in light brown; b TCR A1.9 α-chain in mauve; β-chain grey; c TCR A2.13 α-chain in wheat; β-chain in light green. The TCR CDR 1α, 2α, 3α loops, α -framework, CDR 1β, 2β, 3β loops and β-framework are coloured red, purple, pink, neon-green, gold, magenta, blue, and green, respectively. HIP peptide bound in HLA-DQ8 binding cleft is coloured in lime-green (C-pep portion), and orange (IAPP2 portion). d–f Atomic footprints of TCR A3.10, A1.9, and A2.13 on the surface of HLA-DQ8-HIPL11C, respectively. HLA-DQ8 α- and β-chain are coloured in light-grey, whilst HIPL11C is in dark grey. The CDR loops colours described above. TCR footprint colours are in accordance with the nearest TCR contact residues. The TCRs’ Vα and Vβ centre of mass position are shown as black dots, with the line approximating their docking angle. g–i The pie charts present the relative contribution of each CDR loop, α-, and β-framework of TCR A3.10, A.19 and A2.13 to the surface of HLA-DQ8-HIPL11C, respectively.
