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. 2021 Jun 30;12:698677. doi: 10.3389/fimmu.2021.698677

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Copyright © 2021 Lin and Yan

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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Different binding sites between HLA-G/ILT-2 and HLA-G/ILT-4. ILT-2 residues Tyr38 and Tyr76 bind Phe195 in HLA-G α3 domain, ILT-4 residues Tyr36 and Arg38 bind Phe195–Tyr197 loop in HLA-G α3 domain. (A) ILT-2 binds HLA-G heavy chain associated with β₂m (HLA-G1 and HLA-G5). (B) ILT-4 binds both β₂m-free (HLA-G2 and HLA-G6) and β₂m-associated (HLA-G1 and HLA-G5) HLA-G heavy chain. (C) A panel of novel HLA-G isoforms including isoforms without α1 domain and transmembrane region, or with an extended 5’-region generated by HLA-G mRNA alternative splicing were predicted. However, molecular structure of these novel isoforms and remain to be identified, and interaction with ILTs is unknown yet. and represent ILT-2 and ILT-4 binding site in HLA-G isoforms.

Inline graphic — Different binding sites between HLA-G/ILT-2 and HLA-G/ILT-4. ILT-2 residues Tyr38 and Tyr76 bind Phe195 in HLA-G α3 domain, ILT-4 residues Tyr36 and Arg38 bind Phe195–Tyr197 loop in HLA-G α3 domain. (A) ILT-2 binds HLA-G heavy chain associated with β₂m (HLA-G1 and HLA-G5). (B) ILT-4 binds both β₂m-free (HLA-G2 and HLA-G6) and β₂m-associated (HLA-G1 and HLA-G5) HLA-G heavy chain. (C) A panel of novel HLA-G isoforms including isoforms without α1 domain and transmembrane region, or with an extended 5’-region generated by HLA-G mRNA alternative splicing were predicted. However, molecular structure of these novel isoforms and remain to be identified, and interaction with ILTs is unknown yet. and represent ILT-2 and ILT-4 binding site in HLA-G isoforms.