Fig. 3: Structural overview of the a09b08 TCR in complex with three HBV Env371-379 pHLA-E complexes.
From: Viral sequence determines HLA-E-restricted T cell recognition of hepatitis B surface antigen
a Cartoon overview of the three TCR-pHLA complexes aligned on HLA-E*01:03 (TCR alpha chain in gray, TCR beta chain in green, HLA-E in wheat, B2M is brown, peptides: Env371-379 in magenta, Env371-379 (S3N) in red and Env371-379 (L6I) in blue). b Close-up view of the three TCR-peptide interactions. TCR residues within 4 Å of the peptide are shown as sticks. Dotted lines indicate polar contacts. c Overlay of the three peptides, aligned on HLA-E, showing highly similar conformation in the complexes. d a09b08 TCR contacts to pHLA-E mapped onto the truncated TCR sequence. A wild-type TCR sequence is provided to show the mutations introduced by affinity maturation. CDR residues are underlined and residues within 4.1 Å of the peptide are highlighted in bold with peptide positions indicated below. Residues highlighted in blue and orange indicate positions that are within 4.1 Å of the HLA-E helix 1 and HLA-E helix 2, respectively. e a09b08 TCR contacts to peptide mapped onto the peptide sequences. Peptide residues within 4.1 Å of the TCR alpha chain are highlighted gray, and those of the TCR beta chain are colored green.
