Fig. 4: TRAV6+ TCR recognition of HLA-DR4Vim-64cit59-71. | Nature Communications

Fig. 4: TRAV6+ TCR recognition of HLA-DR4Vim-64cit59-71.

From: The molecular basis underlying T cell specificity towards citrullinated epitopes presented by HLA-DR4

Fig. 4

a Overall cartoon representation of immune TCR A03 and A07 complexed with HLA-DR4Vim-64cit59-71. The HLA-DR4 α and β chains are coloured in white and brown, respectively. The peptide is coloured in pink sticks. The CDR loops 1α, 2α, and 3α are highlighted in cyan, violet, and light green colour, whereas 1β, 2β, 3β are coloured in blue, purple, and dark green, respectively. The FW α residues are coloured in sand and β residues are coloured in beige. b Top: Surface representation of TCR footprint on pHLA with A03 TCR (left panel) and A07 TCR (right panel). TCR footprint colours are in accordance with the nearest TCR contact residue. The Vα and Vβ centre of mass positions are shown in red and blue spheres, respectively, and connected via a black line. Bottom: Pie charts represent the relative contribution of each CDR loop and FW residues of TCR to the interface with HLA-DR4Vim-64cit59-71. Detailed interactions of A03 TCR between (c) CDR1α, 2α and FW α, (d) CDR3α, (e) CDR1β, 2β, 3β and FW β with HLA-DR4, and (i) peptide interactions are shown. Detailed interactions of A07 TCR between (f) CDR1α, 2α and FW α, (g) CDR3α, (h) CDR3β with HLA-DR4, and (j) peptide are shown.

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