Dynamics of SARS-coronavirus HR2 domain in the prefusion and transition states.
Identifieur interne : 002B33 ( Main/Exploration ); précédent : 002B32; suivant : 002B34Dynamics of SARS-coronavirus HR2 domain in the prefusion and transition states.
Auteurs : Susanna Mcreynolds [États-Unis] ; Shaokai Jiang ; Lijun Rong ; Michael CaffreySource :
- Journal of magnetic resonance (San Diego, Calif. : 1997) [ 1096-0856 ] ; 2009.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Viral Envelope Proteins.
- chemistry : SARS Virus.
- methods : Magnetic Resonance Spectroscopy.
- chemical , ultrastructure : Viral Envelope Proteins.
- Kinetics, Phase Transition, Protein Conformation, Protein Structure, Tertiary.
Abstract
The envelope glycoproteins S1 and S2 of severe acute respiratory syndrome coronavirus (SARS-CoV) mediate viral entry by conformational change from a prefusion state to a postfusion state that enables fusion of the viral and target membranes. In this work we present the characterization of the dynamic properties of the SARS-CoV S2-HR2 domain (residues 1141-1193 of S) in the prefusion and newly discovered transition states by NMR (15)N relaxation studies. The dynamic properties of the different states, which are stabilized under different experimental conditions, extend the current model of viral membrane fusion and give insight into the design of structure-based antagonists of SARS-CoV in particular, as well as other enveloped viruses such as HIV.
DOI: 10.1016/j.jmr.2009.09.012
PubMed: 19819173
Affiliations:
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Le document en format XML
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60607</wicri:regionArea><placeName><region type="state">Illinois</region><settlement type="city">Chicago</settlement></placeName><orgName type="university">Université de l'Illinois à Chicago</orgName></affiliation></author><author><name sortKey="Jiang, Shaokai" sort="Jiang, Shaokai" uniqKey="Jiang S" first="Shaokai" last="Jiang">Shaokai Jiang</name></author><author><name sortKey="Rong, Lijun" sort="Rong, Lijun" uniqKey="Rong L" first="Lijun" last="Rong">Lijun Rong</name></author><author><name sortKey="Caffrey, Michael" sort="Caffrey, Michael" uniqKey="Caffrey M" first="Michael" last="Caffrey">Michael Caffrey</name></author></analytic><series><title level="j">Journal of magnetic resonance (San Diego, Calif. : 1997)</title><idno type="eISSN">1096-0856</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Kinetics</term><term>Magnetic Resonance Spectroscopy (methods)</term><term>Phase Transition</term><term>Protein Conformation</term><term>Protein Structure, Tertiary</term><term>SARS Virus (chemistry)</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (ultrastructure)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique</term><term>Conformation des protéines</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (ultrastructure)</term><term>Spectroscopie par résonance magnétique ()</term><term>Structure tertiaire des protéines</term><term>Transition de phase</term><term>Virus du SRAS ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Magnetic Resonance Spectroscopy</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Kinetics</term><term>Phase Transition</term><term>Protein Conformation</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Conformation des protéines</term><term>Protéines de l'enveloppe virale</term><term>Spectroscopie par résonance magnétique</term><term>Structure tertiaire des protéines</term><term>Transition de phase</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The envelope glycoproteins S1 and S2 of severe acute respiratory syndrome coronavirus (SARS-CoV) mediate viral entry by conformational change from a prefusion state to a postfusion state that enables fusion of the viral and target membranes. In this work we present the characterization of the dynamic properties of the SARS-CoV S2-HR2 domain (residues 1141-1193 of S) in the prefusion and newly discovered transition states by NMR (15)N relaxation studies. The dynamic properties of the different states, which are stabilized under different experimental conditions, extend the current model of viral membrane fusion and give insight into the design of structure-based antagonists of SARS-CoV in particular, as well as other enveloped viruses such as HIV.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Illinois</li></region><settlement><li>Chicago</li></settlement><orgName><li>Université de l'Illinois à Chicago</li></orgName></list><tree><noCountry><name sortKey="Caffrey, Michael" sort="Caffrey, Michael" uniqKey="Caffrey M" first="Michael" last="Caffrey">Michael Caffrey</name><name sortKey="Jiang, Shaokai" sort="Jiang, Shaokai" uniqKey="Jiang S" first="Shaokai" last="Jiang">Shaokai Jiang</name><name sortKey="Rong, Lijun" sort="Rong, Lijun" uniqKey="Rong L" first="Lijun" last="Rong">Lijun Rong</name></noCountry><country name="États-Unis"><region name="Illinois"><name sortKey="Mcreynolds, Susanna" sort="Mcreynolds, Susanna" uniqKey="Mcreynolds S" first="Susanna" last="Mcreynolds">Susanna Mcreynolds</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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