We modeled 3D structures of all SARS-CoV-2 proteins, generating 2,060 models that span 69% of the viral proteome and provide details not available elsewhere. We found that ˜6% of the proteome mimicked human proteins, while ˜7% was implicated in hijacking mechanisms that reverse post-translational modifications, block host translation, and disable host defenses; a further ˜29% self-assembled into heteromeric states that provided insight into how the viral replication and translation complex forms. To make these 3D models more accessible, we devised a structural coverage map, a novel visualization method to show what is-and is not-known about the 3D structure of the viral proteome. We integrated the coverage map into an accompanying online resource (https://aquaria.ws/covid) that can be used to find and explore models corresponding to the 79 structural states identified in this work. The resulting Aquaria-COVID resource helps scientists use emerging structural data to understand the mechanisms underlying coronavirus infection and draws attention to the 31% of the viral proteome that remains structurally unknown or dark.


© 2021 The Authors. Published under the terms of the CC BY 4.0 license

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O'Donoghue, S., Schafferhans, A., Sikta, N., Stolte, C., Kaur, S., Ho, B., Anderson, S., Procter, J., Dallago, C., Bordin, N., Adcock, M. & Rost, B. 2021, 'SARS-CoV-2 structural coverage map reveals viral protein assembly, mimicry, and hijacking mechanisms', Molecular Systems Biology, 17(9), article no: e10079. https://doi.org/10.15252/msb.202010079

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Last updated: 16 June 2022
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