Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus
Identifieur interne : 000360 ( PascalFrancis/Checkpoint ); précédent : 000359; suivant : 000361Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus
Auteurs : Pedro Serrano [États-Unis] ; Margaret A. Johnson [États-Unis] ; Marcius S. Almeida [États-Unis] ; Reto Horst [États-Unis] ; Torsten Herrmann [Suisse] ; Jeremiah S. Joseph [États-Unis] ; Benjamin W. Neuman [États-Unis] ; Vanitha Subramanian [États-Unis] ; Kumar S. Saikatendu [États-Unis] ; Michael J. Buchmeier [États-Unis] ; Raymond C. Stevens [États-Unis] ; Peter Kuhn [États-Unis] ; Kurt Wüthrich [États-Unis]Source :
- Journal of virology [ 0022-538X ] ; 2007.
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Abstract
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 β-strands and two α-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.
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Pascal:07-0500922Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus</title>
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<author><name sortKey="Herrmann, Torsten" sort="Herrmann, Torsten" uniqKey="Herrmann T" first="Torsten" last="Herrmann">Torsten Herrmann</name>
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<series><title level="j" type="main">Journal of virology</title>
<title level="j" type="abbreviated">J. virol.</title>
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<seriesStmt><title level="j" type="main">Journal of virology</title>
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<front><div type="abstract" xml:lang="en">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 β-strands and two α-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.</div>
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<fA08 i1="01" i2="1" l="ENG"><s1>Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus</s1>
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<fA11 i1="01" i2="1"><s1>SERRANO (Pedro)</s1>
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<fA60><s1>P</s1>
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<fC01 i1="01" l="ENG"><s0>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 β-strands and two α-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.</s0>
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<s5>01</s5>
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<s5>05</s5>
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