Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus
Identifieur interne : 000330 ( PascalFrancis/Corpus ); précédent : 000329; suivant : 000331Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus
Auteurs : Pedro Serrano ; Margaret A. Johnson ; Marcius S. Almeida ; Reto Horst ; Torsten Herrmann ; Jeremiah S. Joseph ; Benjamin W. Neuman ; Vanitha Subramanian ; Kumar S. Saikatendu ; Michael J. Buchmeier ; Raymond C. Stevens ; Peter Kuhn ; Kurt WüthrichSource :
- Journal of virology [ 0022-538X ] ; 2007.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
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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ET : | Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus |
AU : | SERRANO (Pedro); JOHNSON (Margaret A.); ALMEIDA (Marcius S.); HORST (Reto); HERRMANN (Torsten); JOSEPH (Jeremiah S.); NEUMAN (Benjamin W.); SUBRAMANIAN (Vanitha); SAIKATENDU (Kumar S.); BUCHMEIER (Michael J.); STEVENS (Raymond C.); KUHN (Peter); WÜTHRICH (Kurt) |
AF : | Departments of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road/La Jolla, California 92037/Etats-Unis (1 aut., 2 aut., 3 aut., 4 aut., 11 aut., 13 aut.); Department of Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road/La Jolla, California 92037/Etats-Unis (1 aut., 2 aut., 3 aut., 13 aut.); Joint Center for Structural Genomics, The Scripps Research Institute, 10550 North Torrey Pines Road/La Jolla, California 92037/Etats-Unis (2 aut., 4 aut., 13 aut.); Institute for Molecular Biology and Biophysics, ETH Zürich/8093 Zürich/Suisse (5 aut.); Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road/La Jolla, California 92037/Etats-Unis (6 aut., 8 aut., 9 aut., 12 aut.); Department of Molecular and Integrative Neurosciences, The Scripps Research Institute, 10550 North Torrey Pines Road/La Jolla, California 92037/Etats-Unis (7 aut., 10 aut.); Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road/La Jolla, California 92037/Etats-Unis (13 aut.) |
DT : | Publication en série; Niveau analytique |
SO : | Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2007; Vol. 81; No. 21; Pp. 12049-12060; Bibl. 46 ref. |
LA : | Anglais |
EA : | 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. |
CC : | 002A05C10 |
FD : | Coronavirus; Structure domaine; Protéine; Aigu; Virologie |
FG : | Coronaviridae; Nidovirales; Virus |
ED : | Coronavirus; Domain structure; Protein; Acute; Virology |
EG : | Coronaviridae; Nidovirales; Virus |
SD : | Coronavirus; Estructura dominio; Proteína; Agudo; Virología |
LO : | INIST-13592.354000162035160510 |
ID : | 07-0500922 |
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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="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name>
<affiliation><inist:fA14 i1="05"><s1>Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road</s1>
<s2>La Jolla, California 92037</s2>
<s3>USA</s3>
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<author><name sortKey="Wuthrich, Kurt" sort="Wuthrich, Kurt" uniqKey="Wuthrich K" first="Kurt" last="Wüthrich">Kurt Wüthrich</name>
<affiliation><inist:fA14 i1="01"><s1>Departments of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road</s1>
<s2>La Jolla, California 92037</s2>
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<sZ>11 aut.</sZ>
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<affiliation><inist:fA14 i1="02"><s1>Department of Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road</s1>
<s2>La Jolla, California 92037</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>13 aut.</sZ>
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</affiliation>
<affiliation><inist:fA14 i1="03"><s1>Joint Center for Structural Genomics, The Scripps Research Institute, 10550 North Torrey Pines Road</s1>
<s2>La Jolla, California 92037</s2>
<s3>USA</s3>
<sZ>2 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>13 aut.</sZ>
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<affiliation><inist:fA14 i1="07"><s1>Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road</s1>
<s2>La Jolla, California 92037</s2>
<s3>USA</s3>
<sZ>13 aut.</sZ>
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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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<term>Coronavirus</term>
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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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<fA14 i1="04"><s1>Institute for Molecular Biology and Biophysics, ETH Zürich</s1>
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<fA14 i1="05"><s1>Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road</s1>
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<fA14 i1="06"><s1>Department of Molecular and Integrative Neurosciences, The Scripps Research Institute, 10550 North Torrey Pines Road</s1>
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<sZ>7 aut.</sZ>
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<server><NO>PASCAL 07-0500922 INIST</NO>
<ET>Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus</ET>
<AU>SERRANO (Pedro); JOHNSON (Margaret A.); ALMEIDA (Marcius S.); HORST (Reto); HERRMANN (Torsten); JOSEPH (Jeremiah S.); NEUMAN (Benjamin W.); SUBRAMANIAN (Vanitha); SAIKATENDU (Kumar S.); BUCHMEIER (Michael J.); STEVENS (Raymond C.); KUHN (Peter); WÜTHRICH (Kurt)</AU>
<AF>Departments of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road/La Jolla, California 92037/Etats-Unis (1 aut., 2 aut., 3 aut., 4 aut., 11 aut., 13 aut.); Department of Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road/La Jolla, California 92037/Etats-Unis (1 aut., 2 aut., 3 aut., 13 aut.); Joint Center for Structural Genomics, The Scripps Research Institute, 10550 North Torrey Pines Road/La Jolla, California 92037/Etats-Unis (2 aut., 4 aut., 13 aut.); Institute for Molecular Biology and Biophysics, ETH Zürich/8093 Zürich/Suisse (5 aut.); Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road/La Jolla, California 92037/Etats-Unis (6 aut., 8 aut., 9 aut., 12 aut.); Department of Molecular and Integrative Neurosciences, The Scripps Research Institute, 10550 North Torrey Pines Road/La Jolla, California 92037/Etats-Unis (7 aut., 10 aut.); Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road/La Jolla, California 92037/Etats-Unis (13 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2007; Vol. 81; No. 21; Pp. 12049-12060; Bibl. 46 ref.</SO>
<LA>Anglais</LA>
<EA>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.</EA>
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