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Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer.

Identifieur interne : 001405 ( Ncbi/Checkpoint ); précédent : 001404; suivant : 001406

Structure 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 Lescar

Source :

RBID : pubmed:16511208

Descripteurs français

English descriptors

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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pubmed:16511208

Le document en format XML

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<nlm:affiliation>School of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore.</nlm:affiliation>
<country xml:lang="fr">Singapour</country>
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<name sortKey="Lee, Hooi Chen" sort="Lee, Hooi Chen" uniqKey="Lee H" first="Hooi Chen" last="Lee">Hooi Chen Lee</name>
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<name sortKey="Wilmouth, Rupert" sort="Wilmouth, Rupert" uniqKey="Wilmouth R" first="Rupert" last="Wilmouth">Rupert Wilmouth</name>
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<name sortKey="Liu, Ding Xiang" sort="Liu, Ding Xiang" uniqKey="Liu D" first="Ding Xiang" last="Liu">Ding Xiang Liu</name>
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<term>Catalytic Domain</term>
<term>Crystallography, X-Ray</term>
<term>Cysteine Endopeptidases (chemistry)</term>
<term>Cysteine Endopeptidases (metabolism)</term>
<term>DNA Fragmentation</term>
<term>Dimerization</term>
<term>Enzyme Inhibitors (chemistry)</term>
<term>Hydrogen-Ion Concentration</term>
<term>Models, Molecular</term>
<term>Models, Statistical</term>
<term>Protein Conformation</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary</term>
<term>SARS Virus (enzymology)</term>
<term>Viral Proteins (chemistry)</term>
<term>Viral Proteins (metabolism)</term>
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<term>Antienzymes ()</term>
<term>Catalyse</term>
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<term>Conformation des protéines</term>
<term>Cristallographie aux rayons X</term>
<term>Cysteine endopeptidases ()</term>
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<term>Domaine catalytique</term>
<term>Fragmentation de l'ADN</term>
<term>Modèles moléculaires</term>
<term>Modèles statistiques</term>
<term>Protéines virales ()</term>
<term>Protéines virales (métabolisme)</term>
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<term>Structure tertiaire des protéines</term>
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<term>Cysteine Endopeptidases</term>
<term>Viral Proteins</term>
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<term>SARS Virus</term>
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<term>Cysteine endopeptidases</term>
<term>Protéines virales</term>
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<term>Hydrogen-Ion Concentration</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>Dimérisation</term>
<term>Domaine catalytique</term>
<term>Fragmentation de l'ADN</term>
<term>Modèles moléculaires</term>
<term>Modèles statistiques</term>
<term>Protéines virales</term>
<term>Sites de fixation</term>
<term>Structure secondaire des protéines</term>
<term>Structure tertiaire des protéines</term>
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<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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