K. Falk et al., ALLELE-SPECIFIC PEPTIDE LIGAND MOTIFS OF HLA-C MOLECULES, Proceedings of the National Academy of Sciences of the United Statesof America, 90(24), 1993, pp. 12005-12009
The consensus motifs of HLA-Cw3, -Cw4, -Cw6, and -Cw7 ligands were det
ermined by pool sequencing. Together with information obtained by sequ
encing of some prominent individual peptides, the results indicate the
following: (i) all four HLA-C molecules are associated with peptides.
(ii) These peptides adhere to allele-specific motifs that are similar
to those of to HLA-A or -B molecules; they have a preferred length of
nine amino acids and an anchor residue at the C terminus. (iii) AH fo
ur HLA-C molecules analyzed exhibit related peptide motifs, although e
ach allelic product shows individual characteristics in fine specifici
ty. (iv) Processing and origin of peptides appear not to be different
from that of other class I molecules. (v) No obvious difference at C-t
erminal position 9 was present in the peptides isolated from the two d
imorphic variants of HLA-C that determine dominant resistance to natur
al killer NK1-specific cells (HLA-Cw4, -Cw6) or to NK2-specific cells
(HLA-Cw3, -Cw7) and that differ in two residues in or near the pocket
at position 9.