7RTD
SARS-CoV-2 Spike-derived peptide S269-277 (YLQPRTFLL) presented by HLA-A*02:01
Summary for 7RTD
Entry DOI | 10.2210/pdb7rtd/pdb |
Descriptor | HLA class I antigen, Beta-2-microglobulin, Spike protein S1, ... (4 entities in total) |
Functional Keywords | human leukocyte antigen, major histocompatibility complex, hla-a2, hla-a*02:01, ylqprtfll, immune system |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 3 |
Total formula weight | 54005.53 |
Authors | Szeto, C.,Nguyen, A.T.,Gras, S. (deposition date: 2021-08-13, release date: 2021-10-13, Last modification date: 2024-10-30) |
Primary citation | Szeto, C.,Nguyen, A.T.,Lobos, C.A.,Chatzileontiadou, D.S.M.,Jayasinghe, D.,Grant, E.J.,Riboldi-Tunnicliffe, A.,Smith, C.,Gras, S. Molecular Basis of a Dominant SARS-CoV-2 Spike-Derived Epitope Presented by HLA-A*02:01 Recognised by a Public TCR. Cells, 10:-, 2021 Cited by PubMed Abstract: The data currently available on how the immune system recognises the SARS-CoV-2 virus is growing rapidly. While there are structures of some SARS-CoV-2 proteins in complex with antibodies, which helps us understand how the immune system is able to recognise this new virus; however, we lack data on how T cells are able to recognise this virus. T cells, especially the cytotoxic CD8+ T cells, are critical for viral recognition and clearance. Here we report the X-ray crystallography structure of a T cell receptor, shared among unrelated individuals (public TCR) in complex with a dominant spike-derived CD8+ T cell epitope (YLQ peptide). We show that YLQ activates a polyfunctional CD8+ T cell response in COVID-19 recovered patients. We detail the molecular basis for the shared TCR gene usage observed in HLA-A*02:01+ individuals, providing an understanding of TCR recognition towards a SARS-CoV-2 epitope. Interestingly, the YLQ peptide conformation did not change upon TCR binding, facilitating the high-affinity interaction observed. PubMed: 34685626DOI: 10.3390/cells10102646 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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