7EA6
Crystal structure of TCR-017 ectodomain
Summary for 7EA6
Entry DOI | 10.2210/pdb7ea6/pdb |
Descriptor | T cell receptor 017 alpha chain, T cell receptor 017 beta chain (3 entities in total) |
Functional Keywords | t cell receptor, immune system |
Biological source | Homo sapiens More |
Total number of polymer chains | 4 |
Total formula weight | 99304.53 |
Authors | Nagae, M.,Yamasaki, S. (deposition date: 2021-03-06, release date: 2021-10-13, Last modification date: 2023-11-29) |
Primary citation | Lu, X.,Hosono, Y.,Nagae, M.,Ishizuka, S.,Ishikawa, E.,Motooka, D.,Ozaki, Y.,Sax, N.,Maeda, Y.,Kato, Y.,Morita, T.,Shinnakasu, R.,Inoue, T.,Onodera, T.,Matsumura, T.,Shinkai, M.,Sato, T.,Nakamura, S.,Mori, S.,Kanda, T.,Nakayama, E.E.,Shioda, T.,Kurosaki, T.,Takeda, K.,Kumanogoh, A.,Arase, H.,Nakagami, H.,Yamashita, K.,Takahashi, Y.,Yamasaki, S. Identification of conserved SARS-CoV-2 spike epitopes that expand public cTfh clonotypes in mild COVID-19 patients. J.Exp.Med., 218:-, 2021 Cited by PubMed Abstract: Adaptive immunity is a fundamental component in controlling COVID-19. In this process, follicular helper T (Tfh) cells are a subset of CD4+ T cells that mediate the production of protective antibodies; however, the SARS-CoV-2 epitopes activating Tfh cells are not well characterized. Here, we identified and crystallized TCRs of public circulating Tfh (cTfh) clonotypes that are expanded in patients who have recovered from mild symptoms. These public clonotypes recognized the SARS-CoV-2 spike (S) epitopes conserved across emerging variants. The epitope of the most prevalent cTfh clonotype, S864-882, was presented by multiple HLAs and activated T cells in most healthy donors, suggesting that this S region is a universal T cell epitope useful for booster antigen. SARS-CoV-2-specific public cTfh clonotypes also cross-reacted with specific commensal bacteria. In this study, we identified conserved SARS-CoV-2 S epitopes that activate public cTfh clonotypes associated with mild symptoms. PubMed: 34647971DOI: 10.1084/jem.20211327 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.18000239315 Å) |
Structure validation
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