Structural basis of biased T cell receptor recognition of an immunodominant HLA-A2 epitope of the SARS-CoV-2 spike protein.

J Biol Chem · 2021 · PMC8352664 · PMID 34384783

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highly significantno p-value reported

Specifically, CDR1α engaged HLA-A2 S269–277 by inserting the key residues Gln37 and Ser38 into the narrow space between the p3-p5 of the peptide and HLA-A2 α2 helix, which is highly significant in the context of the available TRAV-encoded sequence space for CDR1α.

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