id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-293417-oqusfhei	Ma, Yanlin	Structures of the N- and C-terminal domains of MHV-A59 nucleocapsid protein corroborate a conserved RNA-protein binding mechanism in coronavirus	2010-07-01		.txt	text/plain	5142	292	55	The higher resolution provides more detailed structural information than previous reports, showing that the NTD structure from MHV shares a similar overall and topology structure with that of SARS-CoV and IBV, but varies in its potential surface, which indicates a possible difference in RNA-binding module. To gain insight into the precise mechanism of N protein, several crystallographic or NMR structural results were reported, including MHV N-terminal RNA binding domain (residues 60-195) (Grossoehme et al., 2009) , two proteaseresistant domains of the N protein from SARS-CoV (Huang et al., 2004; Luo et al., 2006; Yu et al., 2006; Chen et al., 2007; Saikatendu et al., 2007; Takeda et al., 2008) , and IBV (Beaudette strain and Gray strain) (Fan et al., 2005; Jayaram et al., 2006) . In overall ribbon posture, the high resolution structure of MHV-NTD determined using two forms of crystals with different packing modes is similar to previously reported SARS-CoV and IBV structures, with a remarkable difference in surface electrostatic distribution.	./cache/cord-293417-oqusfhei.txt	./txt/cord-293417-oqusfhei.txt