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. 2020 Nov 22;296:100017. doi: 10.1074/jbc.REV120.013309

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© 2020 The Authors

This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

Human-adaptive receptor-binding variants underlying the 1957 H2N2 and 1968 H3N2 pandemic viruses.A, similar to 1918 H1N1, H2 and H3 HAs feature a single dominant variant (Q226L) enabling binding to human-type receptors and a stabilizing covariant (G228S) that ensures specificity. B, architecture and key structural features of human H1 (pink) and human H2 (lilac). The locations of key amino acid positions are highlighted through depiction of Cα positions as enlarged spheres and via labeling of key residues and secondary structural features. The key 226 and 228 positions in H2/H3 lie in close proximity to D225 in human H1. C, enlarged overlay of the avian (yellow) and human (gray) H3 RBS. Panels (B) and (C) assembled in Pymol (Schrodinger LLC) using PDB IDs: 1RVZ, 3KU6, 1MQM, & 6TZB.