A molecule’s right to choose: how diabetogenic class II MHC products bind peptides
J. Clin. Invest. Hidde L. Ploegh, et al. 115:2077 doi:10.1172/JCI26018 [Go to this article.]

Figure 1
Peptide ligands for the class II MHC products I-A^g7 (mouse) and HLA-DQ8 (human). The central core of the peptide ligand is indicated in b colors; anchor residues are shown in dark blue (at P1, P4, P6) and red (at P9). The amino acid residues preferred at the key anchor positions are indicated in single letter code, with the size of the letter proportional to the frequency of its occurrence. At P9, acidic residues (glutamic acid [E] and aspartic acid [D]) are universally preferred and account for greater than 90% of the amino acid residues found at that position. C-terminal of P9, acidic residues (aspartic acid, glutamic acid) are preferred as well. Their frequencies are shown as a percentage of the total number of peptides analyzed that carry an acidic residue at the indicated position. A, alanine; I, isoleucine; L, leucine; Q, glutamine; S, serine; V, valine.