The composition of the F pocket in HLA-A*74 generates C-terminal promiscuity among its bound peptides.

In this study we sequenced the bound peptides from three alleles belonging to the HLA-A74 group (HLA-A74:04, A74:06 and A74:07) that are distinguished by four polymorphic residues within the peptide-binding region. Our data illustrates that A74:04 exhibits preference for L, M or I at P2 and L, S or P at PΩ, while for A74:07 the P2 anchor prefers L, P or I and the PΩ anchor S, P, L. In contrast A*74:06 features a P2 anchor motif of S or L, while a PΩ anchor could not be defined; however, a preference for polar residues S, T, Q or the charged residue R at the PΩ position could be detected.