Recombinant SARS coronavirus nucleocapsid protein forms a dimer through its C-terminal domain
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چکیده
Running Title: Mapping the dimerization domain of SARS-CoV N protein Department of Biological Sciences and the Cancer Center, † Bindley Biosciences Center, Purdue University, West Lafayette, IN 47907 State Key Lab for Biocontrol, Zhongshan University, Guangzhou, P.R.China To whom correspondence should be addressed: Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1393 Phone: 765-496-3113; FAX: 765-496-1189; Email: [email protected]
منابع مشابه
Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain.
The causative agent of severe acute respiratory syndrome (SARS) is the SARS-associated coronavirus, SARS-CoV. The viral nucleocapsid (N) protein plays an essential role in viral RNA packaging. In this study, recombinant SARS-CoV N protein was shown to be dimeric by analytical ultracentrifugation, size exclusion chromatography coupled with light scattering, and chemical cross-linking. Dimeric N ...
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The main protease (M(pro)) of severe acute respiratory syndrome coronavirus (SARS-CoV) plays an essential role in the extensive proteolytic processing of the viral polyproteins (pp1a and pp1ab), and it is an important target for anti-SARS drug development. It was found that SARS-CoV M(pro) exists in solution as an equilibrium of both monomeric and dimeric forms, and the dimeric form is the enzy...
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The nucleocapsid (N) phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV) packages the viral genome into a helical ribonucleocapsid and plays a fundamental role during viral self-assembly. The N protein consists of two structural domains interspersed between intrinsically disordered regions and dimerizes through the C-terminal structural domain (CTD). A key activity of...
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The N-terminal domain of the coronavirus nucleocapsid (N) protein adopts a fold resembling a right hand with a flexible, positively charged beta-hairpin and a hydrophobic palm. This domain was shown to interact with the genomic RNA for coronavirus infectious bronchitis virus (IBV) and severe acute respiratory syndrome coronavirus (SARS-CoV). Based on its 3D structure, we used site-directed muta...
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تاریخ انتشار 2005