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. 2022 Aug 9;10:861609. doi: 10.3389/fchem.2022.861609

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Copyright © 2022 Sandalova, Sala and Achour.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Replacement of three residues in the HLA-A*02:01-restricted melanoma epitope Mart-1 with unnatural amino acids did not alter the conformation while enhancing binding affinity.Comparison of the crystal structure of the wild-type Mart-1 peptide ELAGIGILTV (1JF1. pdb, grey) with the APL in which p1E, p2A and p10V were modified to phenylglycine, norvaline and PRG, respectively (4WJ5. pdb, green) (Hoppes et al., 2014). Two HLA-A*02:01 residues that interact with the modified residues in the APL are also indicated.