Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7N1A

SARS-CoV-2 YLQ peptide binds to HLA-A2

Summary for 7N1A
Entry DOI10.2210/pdb7n1a/pdb
DescriptorMHC class I antigen, A-2 alpha chain, Beta-2-microglobulin, Spike protein S1, ... (5 entities in total)
Functional Keywordspmhc, sars-cov-2, spike, ylq, immune system
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains6
Total formula weight90420.71
Authors
Wu, D.,Mariuzza, R.A. (deposition date: 2021-05-27, release date: 2021-07-28, Last modification date: 2024-11-20)
Primary citationWu, D.,Kolesnikov, A.,Yin, R.,Guest, J.D.,Gowthaman, R.,Shmelev, A.,Serdyuk, Y.,Dianov, D.V.,Efimov, G.A.,Pierce, B.G.,Mariuzza, R.A.
Structural assessment of HLA-A2-restricted SARS-CoV-2 spike epitopes recognized by public and private T-cell receptors.
Nat Commun, 13:19-19, 2022
Cited by
PubMed Abstract: T cells play a vital role in combatting SARS-CoV-2 and forming long-term memory responses. Whereas extensive structural information is available on neutralizing antibodies against SARS-CoV-2, such information on SARS-CoV-2-specific T-cell receptors (TCRs) bound to their peptide-MHC targets is lacking. Here we determine the structures of a public and a private TCR from COVID-19 convalescent patients in complex with HLA-A2 and two SARS-CoV-2 spike protein epitopes (YLQ and RLQ). The structures reveal the basis for selection of particular TRAV and TRBV germline genes by the public but not the private TCR, and for the ability of the TCRs to recognize natural variants of RLQ but not YLQ. Neither TCR recognizes homologous epitopes from human seasonal coronaviruses. By elucidating the mechanism for TCR recognition of an immunodominant yet variable epitope (YLQ) and a conserved but less commonly targeted epitope (RLQ), this study can inform prospective efforts to design vaccines to elicit pan-coronavirus immunity.
PubMed: 35013235
DOI: 10.1038/s41467-021-27669-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.065 Å)
Structure validation

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon