Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein.
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.
Huang
Qiulong
Q
Global Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Illinois 60064-6098, USA.
Yu
Liping
L
Petros
Andrew M
AM
Gunasekera
Angelo
A
Liu
Zhihong
Z
Xu
Nan
N
Hajduk
Philip
P
Mack
Jamey
J
Fesik
Stephen W
SW
Olejniczak
Edward T
ET
D000818:Animals; D001665:Binding Sites; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D019590:Nucleocapsid Proteins / Q000737:chemistry*; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D012313:RNA / Q000378:metabolism; D045473:Severe acute respiratory syndrome-related coronavirus / Q000737:chemistry*
D008024:Ligands; D019590:Nucleocapsid Proteins; D012313:RNA