id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-328300-zehltghv	Lin, Shing-Yen	Structural Basis for the Identification of the N-Terminal Domain of Coronavirus Nucleocapsid Protein as an Antiviral Target	2014-02-24		.txt	text/plain	6628	345	53	CoVs encode the nucleocapsid (N) protein, a major structural protein that plays multiple roles in the virus replication cycle and forms a ribonucleoprotein complex with the viral RNA through the N protein's N-terminal domain (N-NTD). We report the crystal structures of HCoV-OC43 N-NTD complexed with ribonucleoside 5′-monophosphates as a model for understanding the molecular interactions that govern CoV N-NTD binding to RNA. To begin to elucidate how RNA and the N protein interact, we determined the crystal structure of HCoV-OC43 N-NTD complexed with AMP. These amino acids are sequentially and structurally conserved in other HCoV N proteins ( Figure S2 , Supporting Information); therefore, they are likely essential for RNA recognition and interaction in all coronavirus N proteins. Previous studies indicated that the positively charged amino acid, Arg 106, located at the cleft in the HCoV-OC43 N-NTD structure, is conserved in all CoV N proteins and interacts nonspecifically with the RNA phosphate backbone.	./cache/cord-328300-zehltghv.txt	./txt/cord-328300-zehltghv.txt