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. 2020 Feb 26;204(7):1943–1953. doi: 10.4049/jimmunol.1900915

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Copyright © 2020 by The American Association of Immunologists, Inc.

This article is distributed under The American Association of Immunologists, Inc., Reuse Terms and Conditions for Author Choice articles.

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FIGURE 3. — Structural characterization of NYE_S3 TCR binding to NY-ESO-1_157–165(9V)–HLA-A2. (A) Overall cartoon representation of NYE_S3 TCR–pHLA complex. (B) NY-ESO-1_157–165(9V)–HLA-A2 peptide conformation within the NYE_S3 TCR–containing structure. (C) CDR positions above pHLA surface for NYE_S3. (D) CDR3α and CDR3β stacking against the peptide Ile⁶ side chain. The area depicted by the dashed box is expanded in (E) to highlight specific interactions. (F) Contribution of additional NYE_S3 TCR CDRs to peptide binding. Transparent CDR3α and CDR3β lie in the foreground of this panel.