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From the structures, we found that the peptide binding motifs of RLA-A1 are extremely constraining. Thus, there is a generally restricted peptide selection for RLA-A1 compared to that for human HLA-A*0201. In addition, uncommon residues Gly53, Val55, and Glu56 of RLA-A1 are located between the 3<jats:sub>10<\/jats:sub>helix and \u03b11 helix, which makes the steric position of the 3<jats:sub>10<\/jats:sub>helix in RLA-A1 much closer to the \u03b12 helix than that found in other mammalian MHC class I molecules. This special conformation between the 3<jats:sub>10<\/jats:sub>helix and \u03b11 helix plays a pivotal role in rabbit MHC class I assembly. Our results provide new insights into MHC class I molecule assembly and peptide presentation of domestic mammals. 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