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Summary
| Description | Positions of mutations in the SARS-CoV-2 Omicron variant compared to the original strain, showing amino acid substitutions (yellow), deletions (red), and insertions (green). In this trimeric structure, two monomers (gray and light blue) have their receptor-binding domains in the "down" conformation while one (dark blue) is in the "up" or "open" conformation. "Side" view shows receptor-binding domains at the top of the image; the membrane would be located at the bottom. Mutation data source from WHO. Rendered from PDB: 6VYB. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Walls, A.C., Park, Y.J., Tortorici, M.A., Wall, A., McGuire, A.T., Veesler, D. (2020) Cell 181: 281 PubMed: 32155444 DOI: 10.1016/j.cell.2020.02.058 |
| Date | |
| Source | Own work |
| Author | Opabinia regalis |
| Other versions | See File:Spike omicron mutations top.png for top view |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 04:28, 29 November 2021 | | 1,280 × 960 (665 KB) | Opabinia regalis | {{Information |Description=Positions of mutations in the SARS-CoV-2 Omicron variant compared to the original strain, showing amino acid substitutions (yellow), deletions (red), and insertions (green). In this trimeric structure, two monomers (gray and light blue) have their receptor-binding domains in the "down" conformation while one (dark blue) is in the "up" or "open" conformation. "Side" view shows receptor-binding domains at the top of the image; the membrane would be located at the bott... |
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