Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core.
Identifieur interne : 005399 ( Main/Exploration ); précédent : 005398; suivant : 005400Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core.
Auteurs : Yanhui Xu [République populaire de Chine] ; Zhiyong Lou ; Yiwei Liu ; Hai Pang ; Po Tien ; George F. Gao ; Zihe RaoSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2004.
Descripteurs français
- KwdFr :
- Antiviraux (pharmacologie), Clonage moléculaire, Conformation des protéines, Cristallographie aux rayons X, Dimérisation, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Liaison aux protéines, Modèles moléculaires, Motifs d'acides aminés, Peptides (), Protéines de l'enveloppe virale (), Similitude de séquences d'acides aminés, Structure secondaire des protéines, Séquence d'acides aminés, Virus du SRAS (métabolisme).
- MESH :
- métabolisme : Virus du SRAS.
- pharmacologie : Antiviraux.
- Clonage moléculaire, Conformation des protéines, Cristallographie aux rayons X, Dimérisation, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Liaison aux protéines, Modèles moléculaires, Motifs d'acides aminés, Peptides, Protéines de l'enveloppe virale, Similitude de séquences d'acides aminés, Structure secondaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Antiviral Agents (pharmacology), Cloning, Molecular, Crystallography, X-Ray, Dimerization, Membrane Glycoproteins (chemistry), Models, Molecular, Molecular Sequence Data, Peptides (chemistry), Protein Binding, Protein Conformation, Protein Structure, Secondary, SARS Virus (metabolism), Sequence Homology, Amino Acid, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Peptides, Viral Envelope Proteins.
- chemical , pharmacology : Antiviral Agents.
- metabolism : SARS Virus.
- Amino Acid Motifs, Amino Acid Sequence, Cloning, Molecular, Crystallography, X-Ray, Dimerization, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Protein Structure, Secondary, Sequence Homology, Amino Acid, Spike Glycoprotein, Coronavirus.
Abstract
Severe acute respiratory syndrome coronavirus is a newly emergent virus responsible for a recent outbreak of an atypical pneumonia. The coronavirus spike protein, an enveloped glycoprotein essential for viral entry, belongs to the class I fusion proteins and is characterized by the presence of two heptad repeat (HR) regions, HR1 and HR2. These two regions are understood to form a fusion-active conformation similar to those of other typical viral fusion proteins. This hairpin structure likely juxtaposes the viral and cellular membranes, thus facilitating membrane fusion and subsequent viral entry. The fusion core protein of severe acute respiratory syndrome coronavirus spike protein was crystallized, and the structure was determined at 2.8 A of resolution. The fusion core is a six-helix bundle with three HR2 helices packed against the hydrophobic grooves on the surface of central coiled coil formed by three parallel HR1 helices in an oblique antiparallel manner. This structure shares significant similarity with the fusion core structure of mouse hepatitis virus spike protein and other viral fusion proteins, suggesting a conserved mechanism of membrane fusion. Drug discovery strategies aimed at inhibiting viral entry by blocking hairpin formation, which have been successfully used in human immunodeficiency virus 1 inhibitor development, may be applicable to the inhibition of severe acute respiratory syndrome coronavirus on the basis of structural information provided here. The relatively deep grooves on the surface of the central coiled coil will be a good target site for the design of viral fusion inhibitors.
DOI: 10.1074/jbc.M408782200
PubMed: 15345712
Affiliations:
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Le document en format XML
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Gao</name></author><author><name sortKey="Rao, Zihe" sort="Rao, Zihe" uniqKey="Rao Z" first="Zihe" last="Rao">Zihe Rao</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Antiviral Agents (pharmacology)</term><term>Cloning, Molecular</term><term>Crystallography, X-Ray</term><term>Dimerization</term><term>Membrane Glycoproteins (chemistry)</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Peptides (chemistry)</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>SARS Virus (metabolism)</term><term>Sequence Homology, Amino Acid</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antiviraux (pharmacologie)</term><term>Clonage moléculaire</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Motifs d'acides aminés</term><term>Peptides ()</term><term>Protéines de l'enveloppe virale ()</term><term>Similitude de séquences d'acides aminés</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptides</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antiviraux</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Cloning, Molecular</term><term>Crystallography, X-Ray</term><term>Dimerization</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Sequence Homology, Amino Acid</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Motifs d'acides aminés</term><term>Peptides</term><term>Protéines de l'enveloppe virale</term><term>Similitude de séquences d'acides aminés</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus is a newly emergent virus responsible for a recent outbreak of an atypical pneumonia. The coronavirus spike protein, an enveloped glycoprotein essential for viral entry, belongs to the class I fusion proteins and is characterized by the presence of two heptad repeat (HR) regions, HR1 and HR2. These two regions are understood to form a fusion-active conformation similar to those of other typical viral fusion proteins. This hairpin structure likely juxtaposes the viral and cellular membranes, thus facilitating membrane fusion and subsequent viral entry. The fusion core protein of severe acute respiratory syndrome coronavirus spike protein was crystallized, and the structure was determined at 2.8 A of resolution. The fusion core is a six-helix bundle with three HR2 helices packed against the hydrophobic grooves on the surface of central coiled coil formed by three parallel HR1 helices in an oblique antiparallel manner. This structure shares significant similarity with the fusion core structure of mouse hepatitis virus spike protein and other viral fusion proteins, suggesting a conserved mechanism of membrane fusion. Drug discovery strategies aimed at inhibiting viral entry by blocking hairpin formation, which have been successfully used in human immunodeficiency virus 1 inhibitor development, may be applicable to the inhibition of severe acute respiratory syndrome coronavirus on the basis of structural information provided here. The relatively deep grooves on the surface of the central coiled coil will be a good target site for the design of viral fusion inhibitors.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><noCountry><name sortKey="Gao, George F" sort="Gao, George F" uniqKey="Gao G" first="George F" last="Gao">George F. Gao</name><name sortKey="Liu, Yiwei" sort="Liu, Yiwei" uniqKey="Liu Y" first="Yiwei" last="Liu">Yiwei Liu</name><name sortKey="Lou, Zhiyong" sort="Lou, Zhiyong" uniqKey="Lou Z" first="Zhiyong" last="Lou">Zhiyong Lou</name><name sortKey="Pang, Hai" sort="Pang, Hai" uniqKey="Pang H" first="Hai" last="Pang">Hai Pang</name><name sortKey="Rao, Zihe" sort="Rao, Zihe" uniqKey="Rao Z" first="Zihe" last="Rao">Zihe Rao</name><name sortKey="Tien, Po" sort="Tien, Po" uniqKey="Tien P" first="Po" last="Tien">Po Tien</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Xu, Yanhui" sort="Xu, Yanhui" uniqKey="Xu Y" first="Yanhui" last="Xu">Yanhui Xu</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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