The 2C T cell is a CD8+, alloreactive T cell, which recognizes cells bearing Ld and Kbm3 class I major histocompatability complex molecules. Here, we characterize an allopeptide, designated dEV-8, that is a ligand in the Kbm3 molecule for the 2C TCR but is not a ligand in the Ld molecule. By biochemical and immunological properties, dEV-8 is distinct from P2Ca, the Ld allopeptide that is also recognized by the 2C TCR. Using the deduced amino acid sequence of dEV-8, we isolate a candidate endogenous source of the peptide. The endogenous protein, MLRQ, contains a peptide sequence identical to dEV-8. This degenerate recognition of two distinct peptide/MHC complexes by a single TCR has important implications for understanding allorecognition.
A single T cell receptor recognizes structurally distinct MHC/peptide complexes with high specificity.
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M D Tallquist, T J Yun, L R Pease; A single T cell receptor recognizes structurally distinct MHC/peptide complexes with high specificity.. J Exp Med 1 September 1996; 184 (3): 1017–1026. doi: https://doi.org/10.1084/jem.184.3.1017
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