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Recognition of multiple peptide cores by a single t cell receptor.
| Content Provider | CiteSeerX |
|---|---|
| Author | Navreet K., N. Arzoo, Karo K. Geysen, H. Mario Sette, Ro Sercarz, Eli E. |
| Abstract | 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. T CRs recognize an antigen only when the antigen's peptide fragments are lodged in a groovelike site on MHC molecules (1). How do the TCRs interact with the peptide-MHC complex? The answer is not clear because the crystal structure of the TCR-peptide-MHC complex still has not been solved. In the meantime, several models for the ternary |
| File Format | |
| Access Restriction | Open |
| Subject Keyword | Single Cell Receptor Multiple Peptide Core Peptide-mhc Complex Mhc Molecule Present Evidence Alternative Peptide-mhc Ligand Major Histocompatibility Complex Groovelike Site Crystal Structure Contact Residue Peptide Ligand Distinct Core Structure Multiple Set Distinct Core Residue Peptide Fragment Cell Receptor Single Cell Clone Multisubsite Structure Tcr-peptide-mhc Complex Tcrs Interact Several Model |
| Content Type | Text |
