Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer.
Identifieur interne : 002323 ( PubMed/Curation ); précédent : 002322; suivant : 002324Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer.
Auteurs : Ting Xu [Singapour] ; Amy Ooi ; Hooi Chen Lee ; Rupert Wilmouth ; Ding Xiang Liu ; Julien LescarSource :
- Acta crystallographica. Section F, Structural biology and crystallization communications [ 1744-3091 ] ; 2005.
Descripteurs français
- KwdFr :
- Antienzymes (), Catalyse, Concentration en ions d'hydrogène, Conformation des protéines, Cristallographie aux rayons X, Cysteine endopeptidases (), Cysteine endopeptidases (métabolisme), Dimérisation, Domaine catalytique, Fragmentation de l'ADN, Modèles moléculaires, Modèles statistiques, Protéines virales (), Protéines virales (métabolisme), Sites de fixation, Structure secondaire des protéines, Structure tertiaire des protéines, Virus du SRAS (enzymologie).
- MESH :
- enzymologie : Virus du SRAS.
- métabolisme : Cysteine endopeptidases, Protéines virales.
- Antienzymes, Catalyse, Concentration en ions d'hydrogène, Conformation des protéines, Cristallographie aux rayons X, Cysteine endopeptidases, Dimérisation, Domaine catalytique, Fragmentation de l'ADN, Modèles moléculaires, Modèles statistiques, Protéines virales, Sites de fixation, Structure secondaire des protéines, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Binding Sites, Catalysis, Catalytic Domain, Crystallography, X-Ray, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (metabolism), DNA Fragmentation, Dimerization, Enzyme Inhibitors (chemistry), Hydrogen-Ion Concentration, Models, Molecular, Models, Statistical, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, SARS Virus (enzymology), Viral Proteins (chemistry), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Enzyme Inhibitors, Viral Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Viral Proteins.
- enzymology : SARS Virus.
- Binding Sites, Catalysis, Catalytic Domain, Crystallography, X-Ray, DNA Fragmentation, Dimerization, Hydrogen-Ion Concentration, Models, Molecular, Models, Statistical, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary.
Abstract
The 34 kDa main proteinase (Mpro) from the severe acute respiratory syndrome coronavirus (SARS-CoV) plays an important role in the virus life cycle through the specific processing of viral polyproteins. As such, SARS-CoV Mpro is a key target for the identification of specific inhibitors directed against the SARS virus. With a view to facilitating the development of such compounds, crystals were obtained of the enzyme at pH 6.5 in the orthorhombic space group P2(1)2(1)2 that diffract to a resolution of 1.9 A. These crystals contain one monomer per asymmetric unit and the biologically active dimer is generated via the crystallographic twofold axis. The conformation of the catalytic site indicates that the enzyme is active in the crystalline form and thus suitable for structure-based inhibition studies.
DOI: 10.1107/S1744309105033257
PubMed: 16511208
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<term>Cysteine Endopeptidases (chemistry)</term>
<term>Cysteine Endopeptidases (metabolism)</term>
<term>DNA Fragmentation</term>
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<term>Enzyme Inhibitors (chemistry)</term>
<term>Hydrogen-Ion Concentration</term>
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<term>Models, Statistical</term>
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<term>Catalyse</term>
<term>Concentration en ions d'hydrogène</term>
<term>Conformation des protéines</term>
<term>Cristallographie aux rayons X</term>
<term>Cysteine endopeptidases ()</term>
<term>Cysteine endopeptidases (métabolisme)</term>
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<term>Domaine catalytique</term>
<term>Fragmentation de l'ADN</term>
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<term>Protéines virales ()</term>
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<term>Structure secondaire des protéines</term>
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<term>DNA Fragmentation</term>
<term>Dimerization</term>
<term>Hydrogen-Ion Concentration</term>
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<term>Models, Statistical</term>
<term>Protein Conformation</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary</term>
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<term>Catalyse</term>
<term>Concentration en ions d'hydrogène</term>
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<term>Cristallographie aux rayons X</term>
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<term>Dimérisation</term>
<term>Domaine catalytique</term>
<term>Fragmentation de l'ADN</term>
<term>Modèles moléculaires</term>
<term>Modèles statistiques</term>
<term>Protéines virales</term>
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<front><div type="abstract" xml:lang="en">The 34 kDa main proteinase (Mpro) from the severe acute respiratory syndrome coronavirus (SARS-CoV) plays an important role in the virus life cycle through the specific processing of viral polyproteins. As such, SARS-CoV Mpro is a key target for the identification of specific inhibitors directed against the SARS virus. With a view to facilitating the development of such compounds, crystals were obtained of the enzyme at pH 6.5 in the orthorhombic space group P2(1)2(1)2 that diffract to a resolution of 1.9 A. These crystals contain one monomer per asymmetric unit and the biologically active dimer is generated via the crystallographic twofold axis. The conformation of the catalytic site indicates that the enzyme is active in the crystalline form and thus suitable for structure-based inhibition studies.</div>
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<Abstract><AbstractText>The 34 kDa main proteinase (Mpro) from the severe acute respiratory syndrome coronavirus (SARS-CoV) plays an important role in the virus life cycle through the specific processing of viral polyproteins. As such, SARS-CoV Mpro is a key target for the identification of specific inhibitors directed against the SARS virus. With a view to facilitating the development of such compounds, crystals were obtained of the enzyme at pH 6.5 in the orthorhombic space group P2(1)2(1)2 that diffract to a resolution of 1.9 A. These crystals contain one monomer per asymmetric unit and the biologically active dimer is generated via the crystallographic twofold axis. The conformation of the catalytic site indicates that the enzyme is active in the crystalline form and thus suitable for structure-based inhibition studies.</AbstractText>
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