| First Author | Tallquist MD | Year | 1996 |
| Journal | J Exp Med | Volume | 184 |
| Issue | 3 | Pages | 1017-26 |
| PubMed ID | 9064319 | Mgi Jnum | J:35243 |
| Mgi Id | MGI:82695 | Doi | 10.1084/jem.184.3.1017 |
| Citation | Tallquist MD, et al. (1996) A single T cell receptor recognizes structurally distinct MHC/peptide complexes with high specificity. J Exp Med 184(3):1017-26 |
| abstractText | 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. |
