5JHD
Crystal structure of LS10-TCR/M1-HLA-A*02 complex
Summary for 5JHD
| Entry DOI | 10.2210/pdb5jhd/pdb |
| Related | 5ISZ |
| Descriptor | HLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, Influenza M1(58-66) peptide, ... (7 entities in total) |
| Functional Keywords | tcr-hla*a2, m1, influenza, matrix protein, immune system |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 10 |
| Total formula weight | 192641.90 |
| Authors | Stern, L.J.,Selin, L.K.,Song, I. (deposition date: 2016-04-20, release date: 2017-03-01, Last modification date: 2024-11-06) |
| Primary citation | Song, I.,Gil, A.,Mishra, R.,Ghersi, D.,Selin, L.K.,Stern, L.J. Broad TCR repertoire and diverse structural solutions for recognition of an immunodominant CD8(+) T cell epitope. Nat. Struct. Mol. Biol., 24:395-406, 2017 Cited by PubMed Abstract: A keystone of antiviral immunity is CD8 T cell recognition of viral peptides bound to MHC-I proteins. The recognition modes of individual T cell receptors (TCRs) have been studied in some detail, but the role of TCR variation in providing a robust response to viral antigens is unclear. The influenza M1 epitope is an immunodominant target of CD8 T cells that help to control influenza in HLA-A2 individuals. Here we show that CD8 T cells use many distinct TCRs to recognize HLA-A2-M1, which enables the use of different structural solutions to the problem of specifically recognizing a relatively featureless peptide antigen. The vast majority of responding TCRs target a small cleft between HLA-A2 and the bound M1 peptide. These broad repertoires lead to plasticity in antigen recognition and protection against T cell clonal loss and viral escape. PubMed: 28250417DOI: 10.1038/nsmb.3383 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.46 Å) |
Structure validation
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