A single T cell receptor recognizes structurally distinct MHC/peptide complexes with high specificity
| Autor: | T J Yun, Larry R. Pease, M D Tallquist |
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| Rok vydání: | 1996 |
| Předmět: |
Isoantigens
animal structures T cell Immunology Molecular Sequence Data Receptors Antigen T-Cell Peptide Biology Major histocompatibility complex Peptide Mapping Substrate Specificity Mice Sequence Homology Nucleic Acid medicine Immunology and Allergy Animals Humans Amino Acid Sequence Peptide sequence Chromatography High Pressure Liquid chemistry.chemical_classification Base Sequence T-cell receptor Histocompatibility Antigens Class I Articles MHC restriction Ligand (biochemistry) Molecular biology Cell biology Mice Inbred C57BL medicine.anatomical_structure chemistry embryonic structures biology.protein Cattle CD8 |
| Zdroj: | The Journal of Experimental Medicine |
| ISSN: | 0022-1007 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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