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. Author manuscript; available in PMC: 2011 Jul 1.
Published in final edited form as: Mucosal Immunol. 2010 Aug 25;4(1):112–120. doi: 10.1038/mi.2010.44

Figure 1. Primary amino acid sequence alignment of human DQ2-, DR2- and DP2-derived RTLs.

Figure 1

“Empty” rDQ2.5 (RTL800) was derived from DQ2 (DQA1*0501/DQB1*0201), RTL302 from DR2 (DRA1*0101/DRB1*1501), and RTL600 from DP2 (DPA1*0103/DPB1*0201) primary sequences. Gaps in the sequences for optimal alignment (*) and the beta-1//alpha-1 junction (←|→) are shown. The conserved cysteines that form a disulfide bond are shaded yellow, and the cysteine residue present in DQ2-derived RTL800 that has been changed to Serine in RTL801 to prevent intermolecular disulfide bond formation and aggregation is underlined. Genes encoding RTL802 & RTL803, variants of 800 and 801, respectively, encode proteins that have the amino-terminal peptide sequence (MFPQPELPYPQPGSGSGSGSGSGSGSGS) instead of the starting methionine. These molecules bear antigenic α2-gliadin-61-71 (Q65E) “α-II” peptide and linker (the gliadin-derived sequence is underlined).