@article{ODonoghue_S-2021_44943,
title = {SARS-CoV-2 structural coverage map reveals viral protein assembly, mimicry, and hijacking mechanisms},
author = {O'Donoghue, S. and Schafferhans, A. and Sikta, N. and Stolte, C. and Kaur, S. and Ho, B. and Anderson, S. and Procter, J. and Dallago, C. and Bordin, N. and Adcock, M. and Rost, B.},
month = {sep},
year = {2021},
abstract = {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.},
volume = {17},
issue = {9},
journal = {Molecular Systems Biology},
publisher = {Embopress},
url = {https://doi.org/10.15252/msb.202010079},
}
