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. 2018 Nov 8;9:4693. doi: 10.1038/s41467-018-07109-w

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — HLA-B*57:01, HLA-B*57:03 and HLA-B*58:01 present peptides in distinct conformations. a–c The electrostatic potential mapped to the surface of the structures of HLA-B*57:01, HLA-B*57:03 and HLA-B*58:01 respectively (red—electronegative, blue—electropositive). The α1 and α2 helices and the positions of peptide-binding pockets A–F are shown. d–f Superposition of the crystal structures of the LTVQVARVW, LSSPVTKSW and LTVQVARVY peptides (respectively) in complex with HLA-B*57:01 (grey), B*57:03 (cyan) and B*58:01 (orange). The α2 helix has been removed for clarity. g The interaction between the P7Arg (from the peptide LTVQVARVW) and Asp114 in HLA-B*57:01. h The interaction between the P7Arg (from the peptide LTVQVARVW) and Asp114 in HLA-B*58:01. i Superposition of the LTVQVARVW peptides in complex with HLA-B*57:01 (grey) and B*57:03 (cyan). The presence of the Ser116Tyr micropolymorphism (HLA-B*57:01–>HLA-B*57:03) prevents the binding of the P7Arg in the E pocket of HLA-B*57:03