The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor
Open accessAbstract
A newly identified severe acute respiratory syndrome coronavirus (SARS-CoV), is the etiological agent responsible for the outbreak of SARS. The SARS-CoV main protease, which is a 33.8-kDa protease (also called the 3C-like protease), plays a pivotal role in mediating viral replication and transcription functions through extensive proteolytic processing of two replicase polyproteins, pp1a (486 kDa) and pp1ab (790 kDa). Here, we report the crystal structures of the SARS-CoV main protease at different pH values and in complex with a specific inhibitor. The protease structure has a fold that can be described as an augmented serine-protease, but with a Cys-His at the active site. This series of crystal structures, which is the first, to our knowledge, of any protein from the SARS virus, reveal substantial pH-dependent conformational changes, and an unexpected mode of inhibitor binding, providing a structural basis for rational drug design.
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Cited by
A SARS-CoV-2 protein interaction map reveals targets for drug repurposing
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Metadata
- Authors
- Yang, H., Yang, M., Ding, Y., Liu, Y., Lou, Z., Zhou, Z., Sun, L., Mo, L., Ye, S., Pang, H., Gao, G. F., Anand, K., Bartlam, M., Hilgenfeld, R., & Rao, Z.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-10-29
- Volume
- 100
- Issue
- 23
- Pages
- 13190-13195
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2158812536
- Cited by
- 990
- References
- 16
- FWCI
- 29.15
- Type
- journal article
- Language
- en
- Open access
- green
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- Yang, H., Yang, M., Ding, Y., Liu, Y., Lou, Z., Zhou, Z., Sun, L., Mo, L., Ye, S., Pang, H., Gao, G. F., Anand, K., Bartlam, M., Hilgenfeld, R., & Rao, Z. (2003). The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1835675100
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