| Literature DB >> 15147189 |
Qiulong Huang1, Liping Yu, Andrew M Petros, Angelo Gunasekera, Zhihong Liu, Nan Xu, Philip Hajduk, Jamey 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.Entities:
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Year: 2004 PMID: 15147189 DOI: 10.1021/bi036155b
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162