Here, we focussed on 11 additional amino acid residues in TCR-β that showed a highly significant enrichment in the ‘dominant’ library, were distal to the CDR1, 2 and 3 loops ( Figures 1A, B ), and based on TCR structural modelling were predicted to affect the stability of the Vβ domain.
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Modifications outside CDR1, 2 and 3 of the TCR variable β domain increase TCR expression and antigen-specific function.
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