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The 2C TCR represents an excellent model system for examining TCR cross-reactivity because it recognizes two well-characterized and distinct pMHC ligands as strong agonists. The 2C clone was originally isolated as an alloreactive T cell that recognizes Ld as a foreign MHC (23). 2C binds to and is activated by octamer and nonomer peptide fragments of the enzyme α-ketoglutarate dehydrogenase, called p2Ca and QL9, respectively, when bound to Ld (24, 25). Additionally, 2C is positively selected on Kb, and a synthetic peptide called SIY acts as a strong agonist when bound to Kb (26). The Ld-binding peptide QL9 (QLSPFPFDL) and the Kb-binding peptide SIY (SIYRYYGL) share no sequence identity other than a C-terminal leucine, and although Ld and Kb are both murine class I MHC molecules, they differ by 31 residues in the α1α2 domains, making these two ligands for the 2C TCR quite diverse. T cell lines were generated previously by transfection of the 58−/-T cell hybridoma with the 2C TCR or high-affinity mutant m6, m13, or m67 TCR.
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