Homology modelling is widely used in many areas of structure-based analysis and study [37, 38] . However, there are few studies of chicken MHC class I molecules compared with those of human or mouse. The only chicken MHC class I molecule structure that has been solved is the B21 haplotype [18] . Thus, there is little information available on the structure and function of chicken MHC class I molecules. Therefore, the current study used homology modelling to investigate the peptide-binding domains of chicken MHC class I molecules belonging to the B4, B12, B15 and B19 haplotypes. To the best of our knowledge, this is the first attempt to understand the peptide-binding properties of these molecules based on their structures. The assessment indicated that the models were of high quality in terms of their folding and they were suitable for structure-based T cell epitope prediction. The structural characteristics of the peptide-binding properties of these MHC class I molecules were described in the results section. Only four haplotypes with known motifs were selected in this study. However, it is possible to use this solution to predict T cell epitopes of MHC class I molecules belonging to different haplotypes for other antigens in chickens, because the only difference would be the increased number of peptides required for molecular docking.