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. 2022 Feb 28;13:820881. doi: 10.3389/fimmu.2022.820881

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Copyright © 2022 Wei, Li, Wang, Feng, Xie, Li and Zhang

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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The peptide N-terminal extension mode of the MHC-I family. (A) The consistent mode of the N-terminally extended peptide presented by MHC-I. Comparison of the forces between the A pocket and peptides in SLA-I and HLA-I. (B) Sequence alignment and structural comparison of residue at position 167 in SLA-I, HLA-I and Xela-UAA. The amino acids at position 167 are highlighted by a red pentacle. (C) The in vitro refolding efficiency of SLA-1*13:01 was measured with peptides with different numbers of arginines added to the N-terminus of RW12. The black arrow indicates the peak of the complex.