SrasV1, PubMed, Checkpoint, bibRecord, 001D50

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

Identifieur interne : 001D50 ( PubMed/Checkpoint ); précédent : 001D49; suivant : 001D51

Nuclear 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 ; 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 Wüthrich

Source :

Journal of virology [ 0022-538X ] ; 2007.

RBID : pubmed:17728234

Descripteurs français

English descriptors

KwdEn :
- 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), RNA Replicase (metabolism), RNA, Viral (chemistry), SARS Virus (metabolism), Sequence Homology, Amino Acid, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (metabolism), Viral Proteins (chemistry).
MESH :
- chemical , chemistry : RNA Replicase, RNA, Viral, Viral Nonstructural Proteins, Viral Proteins.
- chemical , metabolism : RNA Replicase, Viral Nonstructural Proteins.
- metabolism : SARS Virus.
- methods : Magnetic Resonance Spectroscopy.
- Amino Acid Sequence, Dose-Response Relationship, Drug, Mass Spectrometry, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid.

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 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.

DOI: 10.1128/JVI.00969-07
PubMed: 17728234

Affiliations:

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Le document en format XML

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<term>Molecular Sequence Data</term>
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<term>Modèles moléculaires</term>
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<term>Protéines virales non structurales ()</term>
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<term>Conformation moléculaire</term>
<term>Données de séquences moléculaires</term>
<term>Modèles moléculaires</term>
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<term>Protéines virales non structurales</term>
<term>RNA replicase</term>
<term>Relation dose-effet des médicaments</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Spectrométrie de masse</term>
<term>Spectroscopie par résonance magnétique</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 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.</div>
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<Abstract><AbstractText>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.</AbstractText>
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Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.

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

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