5ISZ

Crystal structure of LS01-TCR/M1-HLA-A*02 complex

Summary for 5ISZ

• Entry DOI: 10.2210/pdb5isz/pdb
• Descriptor: HLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, influenza M1 for 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: 5
• Total formula weight: 94306.55

Authors

Stern, L.J.,Selin, L.K.,Song, I. (deposition date: 2016-03-15, release date: 2017-03-01, Last modification date: 2024-11-20)

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

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: 28250417
DOI: 10.1038/nsmb.3383

Experimental method

X-RAY DIFFRACTION (2.06 Å)