Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein

Biochemistry. 2004 May 25;43(20):6059-63. doi: 10.1021/bi036155b.

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.

MeSH terms

  • Animals
  • Binding Sites
  • Humans
  • Ligands
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Nuclear Magnetic Resonance, Biomolecular
  • Nucleocapsid Proteins / chemistry*
  • Protein Folding
  • Protein Structure, Tertiary*
  • RNA / metabolism
  • Severe acute respiratory syndrome-related coronavirus / chemistry*

Substances

  • Ligands
  • Nucleocapsid Proteins
  • RNA

Associated data

  • PDB/1SSK
  • SWISSPROT/P59595