Crystallization and preliminary crystallographic analysis of the heptad-repeat complex of SARS coronavirus spike protein.
Identifieur interne : 005829 ( Main/Merge ); précédent : 005828; suivant : 005830Crystallization and preliminary crystallographic analysis of the heptad-repeat complex of SARS coronavirus spike protein.
Auteurs : Yanhui Xu [République populaire de Chine] ; Nan Su ; Lan Qin ; Zhihong Bai ; George F. Gao ; Zihe RaoSource :
- Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2004.
Descripteurs français
- KwdFr :
- Concentration en ions d'hydrogène, Conformation des protéines, Cristallisation, Cristallographie aux rayons X, Diffraction des rayons X, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Génome viral, Modèles statistiques, Protéines de fusion virale (), Protéines de l'enveloppe virale (), Structure tertiaire des protéines, Température.
- MESH :
- Concentration en ions d'hydrogène, Conformation des protéines, Cristallisation, Cristallographie aux rayons X, Diffraction des rayons X, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Génome viral, Modèles statistiques, Protéines de fusion virale, Protéines de l'enveloppe virale, Structure tertiaire des protéines, Température.
English descriptors
- KwdEn :
- Crystallization, Crystallography, X-Ray, Genome, Viral, Hydrogen-Ion Concentration, Membrane Fusion, Membrane Glycoproteins (chemistry), Models, Statistical, Protein Conformation, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus, Temperature, Viral Envelope Proteins (chemistry), Viral Fusion Proteins (chemistry), X-Ray Diffraction.
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins, Viral Fusion Proteins.
- Crystallization, Crystallography, X-Ray, Genome, Viral, Hydrogen-Ion Concentration, Membrane Fusion, Models, Statistical, Protein Conformation, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus, Temperature, X-Ray Diffraction.
Abstract
The aetiological agent of an emergent outbreak of atypical pneumonia, severe acute respiratory syndrome (SARS), is a positive-stranded RNA virus (SARS-CoV) belonging to the Coronaviridae family with a genome that differs substantially from those of other known coronaviruses. Highly conserved heptad-repeat (HR1 and HR2) regions in class I viral fusion proteins, including spike protein from SARS coronavirus, interact with each other to form a six-helix bundle, which is called a fusion core. The crystal structure of the fusion core is expected to greatly facilitate drug design. Crystals of the fusion core of SARS-CoV spike protein have been grown at 291 K using PEG 4000 as precipitant. The diffraction pattern of the crystal extends to 2.8 A resolution at 100 K in-house. The crystals have unit-cell parameters a = 121.2, b = 66.3, c = 70.0 A, alpha = gamma = 90, beta = 107.4 degrees and belong to space group C2. Assuming the presence of six molecules per asymmetric unit, the solvent content is estimated to be about 28%.
DOI: 10.1107/S0907444904027258
PubMed: 15583393
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pubmed:15583393Le document en format XML
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<term>Membrane Fusion</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Models, Statistical</term>
<term>Protein Conformation</term>
<term>Protein Structure, Tertiary</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Temperature</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Fusion Proteins (chemistry)</term>
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<term>Diffraction des rayons X</term>
<term>Fusion membranaire</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Génome viral</term>
<term>Modèles statistiques</term>
<term>Protéines de fusion virale ()</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Structure tertiaire des protéines</term>
<term>Température</term>
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<term>Temperature</term>
<term>X-Ray Diffraction</term>
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<term>Cristallisation</term>
<term>Cristallographie aux rayons X</term>
<term>Diffraction des rayons X</term>
<term>Fusion membranaire</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Génome viral</term>
<term>Modèles statistiques</term>
<term>Protéines de fusion virale</term>
<term>Protéines de l'enveloppe virale</term>
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<front><div type="abstract" xml:lang="en">The aetiological agent of an emergent outbreak of atypical pneumonia, severe acute respiratory syndrome (SARS), is a positive-stranded RNA virus (SARS-CoV) belonging to the Coronaviridae family with a genome that differs substantially from those of other known coronaviruses. Highly conserved heptad-repeat (HR1 and HR2) regions in class I viral fusion proteins, including spike protein from SARS coronavirus, interact with each other to form a six-helix bundle, which is called a fusion core. The crystal structure of the fusion core is expected to greatly facilitate drug design. Crystals of the fusion core of SARS-CoV spike protein have been grown at 291 K using PEG 4000 as precipitant. The diffraction pattern of the crystal extends to 2.8 A resolution at 100 K in-house. The crystals have unit-cell parameters a = 121.2, b = 66.3, c = 70.0 A, alpha = gamma = 90, beta = 107.4 degrees and belong to space group C2. Assuming the presence of six molecules per asymmetric unit, the solvent content is estimated to be about 28%.</div>
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