Recognition of multiple peptide cores by a single T cell receptor
| Autor: | Navreet K. Nanda, Alessandro Sette, Eli E. Sercarz, H M Geysen, Karo K. Arzoo |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1995 |
| Předmět: |
Immunology
Molecular Sequence Data Receptors Antigen T-Cell Context (language use) chemical and pharmacologic phenomena Biology Major histocompatibility complex Lymphocyte Activation Mice Structure-Activity Relationship Antigen Immunology and Allergy Animals Amino Acid Sequence Receptor Peptide sequence Hybridomas Sequence Homology Amino Acid Myoglobin T-cell receptor Histocompatibility Antigens Class II Articles MHC restriction Cell biology Biochemistry biology.protein Peptides Sequence Alignment CD8 Protein Binding Signal Transduction |
| Zdroj: | The Journal of Experimental Medicine |
| ISSN: | 1540-9538 0022-1007 |
| Popis: | We present evidence that a single T cell clone can recognize at least five different overlapping peptides, each with its distinct core structure, in the context of the same major histocompatibility complex (MHC) molecule. Distinct core residues are crucial for triggering the T cell receptor (TCR) in each case. These results suggest that the TCR (a) has multiple sets of contact residues for alternative peptide-MHC ligands, the binding to any one of which can trigger the cell; and/or (b) is able to attach to the peptide-MHC complex in more than one orientation. In this sense, the TCR is a multisubsite structure capable of being stimulated by a variety of peptide ligands associated with the same MHC molecules. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|