The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Structural analysis of the SARS-CoV-2 methyltransferase complex involved in RNA cap creation bound to sinefungin
Open accessAbstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the cause of the COVID-19 pandemic. 2′-O-RNA methyltransferase (MTase) is one of the enzymes of this virus that is a potential target for antiviral therapy as it is crucial for RNA cap formation; an essential process for viral RNA stability. This MTase function is associated with the nsp16 protein, which requires a cofactor, nsp10, for its proper activity. Here we show the crystal structure of the nsp10-nsp16 complex bound to the pan-MTase inhibitor sinefungin in the active site. Our structural comparisons reveal low conservation of the MTase catalytic site between Zika and SARS-CoV-2 viruses, but high conservation of the MTase active site between SARS-CoV-2 and SARS-CoV viruses; these data suggest that the preparation of MTase inhibitors targeting several coronaviruses - but not flaviviruses - should be feasible. Together, our data add to important information for structure-based drug discovery.
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Towards automated crystallographic structure refinement with phenix.refine
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Cited by
Structural insights into SARS-CoV-2 proteins
Arya, R., Kumari, S., Pandey, B., Mistry, H., Bihani, S. C., Das, A., Prashar, V., Gupta, G. D., Panicker, L., & Kumar, M. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.11.024 · Cited by 348
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A critical overview of computational approaches employed for COVID-19 drug discovery
Muratov, E. N., Amaro, R., Andrade, C. H., Brown, N., Ekins, S., Fourches, D., Isayev, O., Kozakov, D., Medina-Franco, J. L., Merz, K. M., et al. (2021) · Chemical Society Reviews · doi:10.1039/d0cs01065k · Cited by 206
SARS-CoV-2 Nsp16 activation mechanism and a cryptic pocket with pan-coronavirus antiviral potential
Vithani, N., Ward, M. D., Zimmerman, M. I., Novak, B., Borowsky, J. H., Singh, S., & Bowman, G. R. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.03.024 · Cited by 84
(2023) · doi:10.1038/s41467-023-41312-8 · Cited by 26
Metadata
- Authors
- Krafcikova, P., Silhan, J., Nencka, R., & Boura, E.
- Venue
- Nature Communications
- Published
- 2020-07-24
- Volume
- 11
- Issue
- 1
- Pages
- 3717-3717
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W3045327938
- Cited by
- 269
- References
- 28
- FWCI
- 6.49
- Type
- journal article
- Language
- en
- Open access
- gold
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- Krafcikova, P., Silhan, J., Nencka, R., & Boura, E. (2020). Structural analysis of the SARS-CoV-2 methyltransferase complex involved in RNA cap creation bound to sinefungin. Nature Communications. https://doi.org/10.1038/s41467-020-17495-9
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