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A virus (IAV) causes an acute infection in humans that is normally eliminated by CD8<sup>+</sup> cytotoxic T lymphocytes. Individuals expressing the MHC class I molecule HLA-A2 produce cytotoxic T lymphocytes bearing T-cell receptors (TCRs) that recognize the immunodominant IAV epitope GILGFVFTL (GIL). Most GIL-specific TCRs utilize \u03b1/\u03b2 chain pairs encoded by the TRAV27/TRBV19 gene combination to recognize this relatively featureless peptide epitope (canonical TCRs). However, \u223c40% of GIL-specific TCRs express a wide variety of other TRAV/TRBV combinations (non-canonical TCRs). To investigate the structural underpinnings of this remarkable diversity, we determined the crystal structure of a non-canonical GIL-specific TCR (F50) expressing the TRAV13-1/TRBV27 gene combination bound to GIL-HLA-A2 to 1.7 \u00c5 resolution. Comparison of the F50-GIL-HLA-A2 complex with the previously published complex formed by a canonical TCR (JM22) revealed that F50 and JM22 engage GIL-HLA-A2 in markedly different orientations. These orientations are distinguished by crossing angles of TCR to peptide-MHC of 29\u00b0 for F50 <i>versus</i> 69\u00b0 for JM22 and by a focus by F50 on the C terminus rather than the center of the MHC \u03b11 helix for JM22. In addition, F50, unlike JM22, uses a tryptophan instead of an arginine to fill a critical notch between GIL and the HLA-A2 \u03b12 helix. The F50-GIL-HLA-A2 complex shows that there are multiple structurally distinct solutions to recognizing an identical peptide-MHC ligand with sufficient affinity to elicit a broad anti-IAV response that protects against viral escape and T-cell clonal loss.","bibjson":{"author":[{"initials":"X","lastname":"Yang","name":"Yang X"},{"initials":"G","lastname":"Chen","name":"Chen G"},{"initials":"NP","lastname":"Weng","name":"Weng NP"},{"initials":"RA","lastname":"Mariuzza","name":"Mariuzza RA"}],"identifier":[{"id":"10.1074/jbc.M117.810382","type":"doi"},{"id":"28931605","type":"pubmed"}],"issue":[null],"journal":{"iso_abbreviation":"J. Biol. Chem.","name":""},"pages":[null],"title":"Structural basis for clonal diversity of the human T cell response to a dominant influenza virus epitope.","type":"article","url":"https://www.sciencedirect.com/science/article/abs/pii/S0021925820329781","volume":[null],"year":[2017]},"in_pmc":"N","in_pmce":"Y","open_access":"N"},"resolution":"1.70","same_as":{"pdbe":{"url":"https://www.ebi.ac.uk/pdbe/entry/pdb/5tez"},"rcsb":{"url":"https://www.rcsb.org/structure/5tez"},"stcrdab":{"url":"http://opig.stats.ox.ac.uk/webapps/stcrdab/StrViewer?pdb=5tez"}},"species":{"common_name":"Human","match_type":"histo:assign_species","scientific_name":"Homo sapiens","slug":"homo_sapiens"},"tcr":{"alpha":{"chains":["I"],"subgroup":"TRAV13"},"beta":{"chains":["J"],"subgroup":"TRBV27"},"mhc_type":"class_i","pdb_code":"5tez"},"title":"HLA-A*02:01 presenting \"GILGFVFTL\" to Alpha/Beta T cell receptor at 1.70&#8491; resolution","unique_chain_count":5}}