Solution structure of the severe acute respiratory syndrome-coronavirus heptad repeat 2 domain in the prefusion state.
Identifieur interne : 003C99 ( Main/Exploration ); précédent : 003C98; suivant : 003D00Solution structure of the severe acute respiratory syndrome-coronavirus heptad repeat 2 domain in the prefusion state.
Auteurs : Susanna Hakansson-Mcreynolds [États-Unis] ; Shaokai Jiang ; Lijun Rong ; Michael CaffreySource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2006.
Descripteurs français
- KwdFr :
- Conformation des protéines, Cristallographie aux rayons X, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Glycoprotéines membranaires (synthèse chimique), Humains, Hémagglutinines virales, Modèles moléculaires, Protéines de fusion virale (génétique), Protéines de fusion virale (métabolisme), Protéines de fusion virale (synthèse chimique), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Solubilité, Séquences répétées d'acides aminés (génétique), Virus du SRAS (), Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de fusion virale, Protéines de l'enveloppe virale, Séquences répétées d'acides aminés, Virus du SRAS.
- métabolisme : Glycoprotéines membranaires, Protéines de fusion virale, Protéines de l'enveloppe virale, Virus du SRAS.
- synthèse chimique : Glycoprotéines membranaires, Protéines de fusion virale.
- Conformation des protéines, Cristallographie aux rayons X, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Hémagglutinines virales, Modèles moléculaires, Protéines de l'enveloppe virale, Solubilité, Virus du SRAS.
English descriptors
- KwdEn :
- Crystallography, X-Ray, Hemagglutinins, Viral, Humans, Membrane Glycoproteins (chemical synthesis), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Models, Molecular, Protein Conformation, Repetitive Sequences, Amino Acid (genetics), SARS Virus (chemistry), SARS Virus (genetics), SARS Virus (metabolism), Solubility, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Viral Fusion Proteins (chemical synthesis), Viral Fusion Proteins (genetics), Viral Fusion Proteins (metabolism).
- MESH :
- chemical , chemical synthesis : Membrane Glycoproteins, Viral Fusion Proteins.
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins, Viral Fusion Proteins.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins, Viral Fusion Proteins.
- chemical : Hemagglutinins, Viral, Spike Glycoprotein, Coronavirus.
- chemistry : SARS Virus.
- genetics : Repetitive Sequences, Amino Acid, SARS Virus.
- metabolism : SARS Virus.
- Crystallography, X-Ray, Humans, Models, Molecular, Protein Conformation, Solubility.
Abstract
The envelope glycoprotein, termed the spike protein, of severe acute respiratory syndrome coronavirus (SARS-CoV) is known to mediate viral entry. Similar to other class 1 viral fusion proteins, the heptad repeat regions of SARS-CoV spike are thought to undergo conformational changes from a prefusion form to a subsequent post-fusion form that enables fusion of the viral and host membranes. Recently, the structure of a post-fusion form of SARS-CoV spike, which consists of isolated domains of heptad repeats 1 and 2 (HR1 and HR2), has been determined by x-ray crystallography. To date there is no structural information for the prefusion conformations of SARS-CoV HR1 and HR2. In this work we present the NMR structure of the HR2 domain (residues 1141-1193) from SARS-CoV (termed S2-HR2) in the presence of the co-solvent trifluoroethanol. We find that in the absence of HR1, S2-HR2 forms a coiled coil symmetric trimer with a complex molecular mass of 18 kDa. The S2-HR2 structure, which is the first example of the prefusion form of coronavirus envelope, supports the current model of viral membrane fusion and gives insight into the design of structure-based antagonists of SARS.
DOI: 10.1074/jbc.M601174200
PubMed: 16507566
Affiliations:
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Le document en format XML
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USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois 60607</wicri:regionArea><orgName type="university">Université de l'Illinois à Chicago</orgName><placeName><settlement type="city">Chicago</settlement><region type="state">Illinois</region></placeName></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">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2006" 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Conformation</term><term>Solubility</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Humains</term><term>Hémagglutinines virales</term><term>Modèles moléculaires</term><term>Protéines de l'enveloppe virale</term><term>Solubilité</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The envelope glycoprotein, termed the spike protein, of severe acute respiratory syndrome coronavirus (SARS-CoV) is known to mediate viral entry. Similar to other class 1 viral fusion proteins, the heptad repeat regions of SARS-CoV spike are thought to undergo conformational changes from a prefusion form to a subsequent post-fusion form that enables fusion of the viral and host membranes. Recently, the structure of a post-fusion form of SARS-CoV spike, which consists of isolated domains of heptad repeats 1 and 2 (HR1 and HR2), has been determined by x-ray crystallography. To date there is no structural information for the prefusion conformations of SARS-CoV HR1 and HR2. In this work we present the NMR structure of the HR2 domain (residues 1141-1193) from SARS-CoV (termed S2-HR2) in the presence of the co-solvent trifluoroethanol. We find that in the absence of HR1, S2-HR2 forms a coiled coil symmetric trimer with a complex molecular mass of 18 kDa. The S2-HR2 structure, which is the first example of the prefusion form of coronavirus envelope, supports the current model of viral membrane fusion and gives insight into the design of structure-based antagonists of SARS.</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="Hakansson Mcreynolds, Susanna" sort="Hakansson Mcreynolds, Susanna" uniqKey="Hakansson Mcreynolds S" first="Susanna" last="Hakansson-Mcreynolds">Susanna Hakansson-Mcreynolds</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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