2idy
NMR Structure of the SARS-CoV non-structural protein nsp3a
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OverviewOverview
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.
About this StructureAbout this Structure
2IDY is a Single protein structure of sequence from Sars coronavirus. Full crystallographic information is available from OCA.
ReferenceReference
Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus., Serrano P, Johnson MA, Almeida MS, Horst R, Herrmann T, Joseph JS, Neuman BW, Subramanian V, Saikatendu KS, Buchmeier MJ, Stevens RC, Kuhn P, Wuthrich K, J Virol. 2007 Nov;81(21):12049-60. Epub 2007 Aug 29. PMID:17728234
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