Structure of the N-Terminal RNA-Binding Domain of the SARS CoV Nucleocapsid Protein
Biochemistry2004Vol. 43(20), pp. 6059–6063
Citations Over TimeTop 10% of 2004 papers
Qiulong Huang, Liping Yu, Andrew M. Petros, Angelo Gunasekera, Zhihong Liu, Nan Xu, Philip J. Hajduk, J. Mack, Stephen W. Fesik, Edward T. Olejniczak
Abstract
The severe acute respiratory syndrome (SARS) virus belongs to the Coronaviridea family of viruses. Its virion encodes several proteins including a replicase and four structural proteins. Here we describe the three-dimensional structure of the N-terminal domain of the SARS coronavirus (CoV) nucleocapsid protein. The protein consists of a five-stranded beta sheet with a folding topology distinct from other RNA-binding proteins. Single-stranded RNAs bind to the protein surface at the junction between a flexible, positively charged beta hairpin and the core structure. NMR-based screening was used to identify low molecular weight compounds that bind to this site.
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