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7EA6

Crystal structure of TCR-017 ectodomain

Summary for 7EA6
Entry DOI10.2210/pdb7ea6/pdb
DescriptorT cell receptor 017 alpha chain, T cell receptor 017 beta chain (3 entities in total)
Functional Keywordst cell receptor, immune system
Biological sourceHomo sapiens
More
Total number of polymer chains4
Total formula weight99304.53
Authors
Nagae, M.,Yamasaki, S. (deposition date: 2021-03-06, release date: 2021-10-13, Last modification date: 2023-11-29)
Primary citationLu, 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: 34647971
DOI: 10.1084/jem.20211327
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.18000239315 Å)
Structure validation

226707

数据于2024-10-30公开中

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