Skip to main content
. 2015 Oct 1;290(48):29106–29119. doi: 10.1074/jbc.M115.691311

FIGURE 6.

FIGURE 6.

Models of the RA11 and E4.1 TCRs bound to NLV·HLA-A2. A, the RA11 (16) and E4.1 (12) TCR models are superposed with α chains in cyan, β chains in green, peptide in magenta sticks, and MHCs (visible as a single MHC as backbones are identical) in orange. B, the NNNDM CDR3α motif in the RA11-NLV·HLA-A2 model is compared with the corresponding motif from the C25·NLV·HLA-A2 crystal structure (backbone r.m.s.d. 2.0 Å; TCR and peptide from the C25·NLV·HLA-A2 complex are pink). Residues corresponding to the NNNDM motif are labeled and shown as sticks as well as P4 Pro of the NLV peptide. C, comparison of the hydrophobic region near NLV P5 Met between the modeled RA11 complex and C25·NLV·HLA-A2 (gray). Proximal hydrophobic TCR residues are labeled and shown as sticks. D, positioning of the CDR1α loop and Tyr-31α in the E4.1-NLV·HLA-A2 model (cyan) compared with the C25·NLV·HLA-A2 structure (gray) and the RA11-NLV·HLA-A2 model (yellow).