It has proved that a subset of alloreactive interactions that include allo-MHC–restricted TCR/MHC recognition events is very analogous to self-restricted TCR/MHC interactions and involves high specificity for MHC-bound peptide. NB20 bound its alloligand HLA-A2-CLG with a Kd in the range of self-restricted interactions and did not bind irrelevant HLA-A2 peptides or other class I MHC molecules, consistent with the properties of the NB20 T-cell clone and analogous to self-restricted TCRs. Use of CLG variants underlined the importance of multiple peptide residues in NB20 recognition, most of which (L5, L6, and M8) have large exposed side chains prominently positioned in the alloligand structure, indicating direct interaction. In contrast, CLG recognition was unaffected by P1 substitution in the least prominent section of CLG.
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