Comparison of the H-2Kk- and H-2Kkm1-restricted peptide motifs.
Self-peptide pools eluted from purified H-2Kk or H-2Kkm1 molecules were sequenced. The majority of self-peptides associated with H-2Kk molecules were found to be octamers with two anchor positions. Position 2 is invariantly occupied with Glu, and the C-terminal residue at position 8 is almost always Ile. Comparison of this motif with synthetic peptides known to contain viral or parasite T-cell epitopes could be well aligned with this motif, except that the C-terminal Ile residue frequently appears to be at position 9 of the aligned sequences, instead of 8. Self-peptides eluted from mutant H-2Kkm1 molecules also appear to be mostly octamers with the same Ile residues at position 8 as with Kk. Position 2 is still dominantly occupied by Glu; in contrast to the Kk motif, however, Gln, Gly, and Pro are also allowed. Other differences between the two motifs indicate that a certain number of peptides presented by one of the molecules are not presented by the other.
Norda
M
M
Max-Planck-Institut für Biologie, Abteilung Immungenetik, Tübingen, Germany.
Falk
K
K
Rötzschke
O
O
Stevanović
S
S
Jung
G
G
Rammensee
H G
HG
D000595:Amino Acid Sequence; D000818:Animals; D006183:H-2 Antigens / Q000737:chemistry*; D051379:Mice; D008809:Mice, Inbred C3H; D008808:Mice, Inbred CBA; D008815:Mice, Inbred Strains; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D014407:Tumor Cells, Cultured
D006183:H-2 Antigens; C024755:H-2K(K) antigen; D010455:Peptides