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Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus

Serrano, P., Johnson, M. A., Almeida, M. S., Horst, R., Herrmann, T., Joseph, J. S., Neuman, B. W., Subramanian, V., Saikatendu, K. S., Buchmeier, M. J., Stevens, R. C., Kuhn, P. and Wuthrich, K. (2007) Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus. Journal of Virology, 81 (21). pp. 12049-60. ISSN 0022-538X

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To link to this article DOI: 10.1128/JVI.00969-07

Abstract/Summary

This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. In addition to the four beta-strands and two alpha-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a feature that has not previously been observed in these proteins. Nuclear magnetic resonance chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA. Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences
ID Code:10078
Uncontrolled Keywords:Amino Acid Sequence, Dose-Response Relationship, Drug, Magnetic Resonance Spectroscopy/*methods, Mass Spectrometry, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, RNA Replicase/*chemistry/metabolism, RNA, Viral/chemistry, SARS Virus/*metabolism, Sequence Homology, Amino Acid, Viral Nonstructural Proteins/*chemistry/metabolism, Viral Proteins/chemistry
Additional Information:Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

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