SARS CoV main proteinase: The monomer-dimer equilibrium dissociation constant.
Identifieur interne : 003D40 ( Main/Exploration ); précédent : 003D39; suivant : 003D41SARS CoV main proteinase: The monomer-dimer equilibrium dissociation constant.
Auteurs : Vito Graziano [États-Unis] ; William J. Mcgrath ; Lin Yang ; Walter F. MangelSource :
- Biochemistry [ 0006-2960 ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Virus du SRAS.
- métabolisme : Cysteine endopeptidases, Protéines virales.
- Cinétique, Cysteine endopeptidases, Diffraction des rayons X, Dimérisation, Protéines virales.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Viral Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Viral Proteins.
- enzymology : SARS Virus.
- Dimerization, Kinetics, X-Ray Diffraction.
Abstract
The SARS coronavirus main proteinase (SARS CoV main proteinase) is required for the replication of the severe acute respiratory syndrome coronavirus (SARS CoV), the virus that causes SARS. One function of the enzyme is to process viral polyproteins. The active form of the SARS CoV main proteinase is a homodimer. In the literature, estimates of the monomer-dimer equilibrium dissociation constant, KD, have varied more than 65,0000-fold, from <1 nM to more than 200 microM. Because of these discrepancies and because compounds that interfere with activation of the enzyme by dimerization may be potential antiviral agents, we investigated the monomer-dimer equilibrium by three different techniques: small-angle X-ray scattering, chemical cross-linking, and enzyme kinetics. Analysis of small-angle X-ray scattering data from a series of measurements at different SARS CoV main proteinase concentrations yielded KD values of 5.8 +/- 0.8 microM (obtained from the entire scattering curve), 6.5 +/- 2.2 microM (obtained from the radii of gyration), and 6.8 +/- 1.5 microM (obtained from the forward scattering). The KD from chemical cross-linking was 12.7 +/- 1.1 microM, and from enzyme kinetics, it was 5.2 +/- 0.4 microM. While each of these three techniques can present different, potential limitations, they all yielded similar KD values.
DOI: 10.1021/bi061746y
PubMed: 17144656
Affiliations:
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Le document en format XML
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<term>Dimerization</term>
<term>Kinetics</term>
<term>SARS Virus (enzymology)</term>
<term>Viral Proteins (chemistry)</term>
<term>Viral Proteins (metabolism)</term>
<term>X-Ray Diffraction</term>
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<term>Cysteine endopeptidases ()</term>
<term>Cysteine endopeptidases (métabolisme)</term>
<term>Diffraction des rayons X</term>
<term>Dimérisation</term>
<term>Protéines virales ()</term>
<term>Protéines virales (métabolisme)</term>
<term>Virus du SRAS (enzymologie)</term>
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<term>Viral Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term>
<term>Viral Proteins</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cysteine endopeptidases</term>
<term>Protéines virales</term>
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<term>Kinetics</term>
<term>X-Ray Diffraction</term>
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<term>Cysteine endopeptidases</term>
<term>Diffraction des rayons X</term>
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<front><div type="abstract" xml:lang="en">The SARS coronavirus main proteinase (SARS CoV main proteinase) is required for the replication of the severe acute respiratory syndrome coronavirus (SARS CoV), the virus that causes SARS. One function of the enzyme is to process viral polyproteins. The active form of the SARS CoV main proteinase is a homodimer. In the literature, estimates of the monomer-dimer equilibrium dissociation constant, KD, have varied more than 65,0000-fold, from <1 nM to more than 200 microM. Because of these discrepancies and because compounds that interfere with activation of the enzyme by dimerization may be potential antiviral agents, we investigated the monomer-dimer equilibrium by three different techniques: small-angle X-ray scattering, chemical cross-linking, and enzyme kinetics. Analysis of small-angle X-ray scattering data from a series of measurements at different SARS CoV main proteinase concentrations yielded KD values of 5.8 +/- 0.8 microM (obtained from the entire scattering curve), 6.5 +/- 2.2 microM (obtained from the radii of gyration), and 6.8 +/- 1.5 microM (obtained from the forward scattering). The KD from chemical cross-linking was 12.7 +/- 1.1 microM, and from enzyme kinetics, it was 5.2 +/- 0.4 microM. While each of these three techniques can present different, potential limitations, they all yielded similar KD values.</div>
</front>
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<name sortKey="Mcgrath, William J" sort="Mcgrath, William J" uniqKey="Mcgrath W" first="William J" last="Mcgrath">William J. Mcgrath</name>
<name sortKey="Yang, Lin" sort="Yang, Lin" uniqKey="Yang L" first="Lin" last="Yang">Lin Yang</name>
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<country name="États-Unis"><noRegion><name sortKey="Graziano, Vito" sort="Graziano, Vito" uniqKey="Graziano V" first="Vito" last="Graziano">Vito Graziano</name>
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