The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Structural Basis of Severe Acute Respiratory Syndrome Coronavirus ADP-Ribose-1″-Phosphate Dephosphorylation by a Conserved Domain of nsP3
Open accessAbstract
The crystal structure of a conserved domain of nonstructural protein 3 (nsP3) from severe acute respiratory syndrome coronavirus (SARS-CoV) has been solved by single-wavelength anomalous dispersion to 1.4 Å resolution. The structure of this “X” domain, seen in many single-stranded RNA viruses, reveals a three-layered α/β/α core with a macro-H2A-like fold. The putative active site is a solvent-exposed cleft that is conserved in its three structural homologs, yeast Ymx7, Archeoglobus fulgidus AF1521, and Er58 from E. coli. Its sequence is similar to yeast YBR022W (also known as Poa1P), a known phosphatase that acts on ADP-ribose-1″-phosphate (Appr-1″-p). The SARS nsP3 domain readily removes the 1″ phosphate group from Appr-1″-p in in vitro assays, confirming its phosphatase activity. Sequence and structure comparison of all known macro-H2A domains combined with available functional data suggests that proteins of this superfamily form an emerging group of nucleotide phosphatases that dephosphorylate Appr-1″-p.
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Cites
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C., et al. (2003) · Nature · doi:10.1038/nature02145 · Cited by 5,923
Identification of a novel coronavirus in patients with severe acute respiratory syndrome
Drosten, C., Günther, S., Preiser, W., van der Werf, S., Brodt, H.-R., Becker, S., Rabenau, H., Panning, M., Kolesnikova, L., Fouchier, R. A. M., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030747 · Cited by 4,574
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984 · cited 3×
“Comparison of one of the chains of SARS ADRP against all known structures in the PDB by using DALI (Holm and Sander, 1993) revealed the presence of two structural homologs: a hypothetical protein from Archeoglobus fulgidus, AF1521 (PDB code: 1HJZ; z score of 18.1; rmsd of 2.4 Å for 152 superimposed Ca atoms; pairs wi…”
MethodInfluential
Cited by
Coronaviruses post-SARS: update on replication and pathogenesis
Perlman, S., & Netland, J. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2147 · Cited by 1,764
Báez-Santos, Y. M., St. John, S. E., & Mesecar, A. D. (2015) · Antiviral Research · doi:10.1016/j.antiviral.2014.12.015 · Cited by 854
Ratia, K., Saikatendu, K. S., Santarsiero, B. D., Barretto, N., Baker, S. C., Stevens, R. C., & Mesecar, A. D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510851103 · Cited by 414
Self-citationStructural 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
Drug Development and Medicinal Chemistry Efforts toward SARS‐Coronavirus and Covid‐19 Therapeutics
Ghosh, A. K., Brindisi, M., Shahabi, D., Chapman, M. E., & Mesecar, A. D. (2020) · ChemMedChem · doi:10.1002/cmdc.202000223 · Cited by 306
Metadata
- Authors
- Saikatendu, K. S., Joseph, J. S., Subramanian, V., Clayton, T., Griffith, M., Moy, K., Velasquez, J., Neuman, B. W., Buchmeier, M. J., Stevens, R. C., & Kuhn, P.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2005-11
- Volume
- 13
- Issue
- 11
- Pages
- 1665-1675
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2019184993
- Cited by
- 204
- References
- 3
- FWCI
- 8.87
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Saikatendu, K. S., Joseph, J. S., Subramanian, V., Clayton, T., Griffith, M., Moy, K., Velasquez, J., Neuman, B. W., Buchmeier, M. J., Stevens, R. C., & Kuhn, P. (2005). Structural Basis of Severe Acute Respiratory Syndrome Coronavirus ADP-Ribose-1″-Phosphate Dephosphorylation by a Conserved Domain of nsP3. Structure. https://doi.org/10.1016/j.str.2005.07.022
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
