SrasV1, Main, Exploration, bibRecord, 005398

Crystallization and preliminary crystallographic analysis of the heptad-repeat complex of SARS coronavirus spike protein.

Identifieur interne : 005398 ( Main/Exploration ); précédent : 005397; suivant : 005399

Crystallization 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 Rao

Source :

Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2004.

RBID : pubmed:15583393

Descripteurs français

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

Affiliations:

Le document en format XML

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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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Crystallization and preliminary crystallographic analysis of the heptad-repeat complex of SARS coronavirus spike protein.

Crystallization and preliminary crystallographic analysis of the heptad-repeat complex of SARS coronavirus spike protein.

Source :

Descripteurs français

English descriptors

Abstract

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