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. 2017 Feb 15;15(4):1555–1564. doi: 10.3892/mmr.2017.6206

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Copyright: © Tao et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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Figure 1. — Schematic representation of chimeric TCR variants used in the present study. wtTCRs were isolated from tumor-infiltrating lymphocytes of patients as control TCRs. Three chimeric TCRs constructs were generated by replacement of the either IgC, cp+tm+ic, or C regions of αβTCR (white) by corresponding γδTCR (black). The amino acid boundaries of the domains were as follows: TCR∆IgC α chain (aa132-221) replaced by δ chain (aa140-231), β chain (aa136-263) replaced by γ chain (aa140-248); TCR∆IgC retained the connecting peptide domains of the α and β chains. TCR∆cp+tm+ic α chain (aa222-271) replaced by δ chain (aa232-292), β chain (aa264-313) replaced by γ chain (aa249-311), TCR∆C α chain (aa132-271) replaced by δ chain (aa140-292), β chain (aa136-313) replaced by γ chain (aa140-311). TCR, T cell receptor; wt, wild-type; Ig, immunoglobulin-like; cp+tm+ic, connecting peptide, transmembrane and intracellular; C, complete region.