id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-293375-qcy56ui7	Strauss, Ellen G.	Identification of the active site residues in the nsP2 proteinase of sindbis virus	1992-12-31		.txt	text/plain	5192	265	56	coma-, nepo-, and potyviruses; coronaviruses; and flaviviruses (and their proposed relatives pestiviruses and hepatitis C virus.) Originally these domains were predicted to have proteolytic activity based on the presence of certain conserved amino acid residues and on the basis of protein-modeling studies (Bazan and Fletterick, 1989; Boege et a/., 1981; Gorbalenya et al., 1989; Hahn eta/., 1985) . Furthermore, we present data to show that none of the asparagine residues in the proteinase domain of Sindbis nsP2 that are conserved among alphaviruses are absolutely required for proteolytic activity, but that Trp-559, adjacent to His-558, is essential for function. We also examined the effect of changing Cys-525, one of the two remaining conserved cysteine residues in the C-terminal half of nsP2, to serine or arginine, as well as changing Ser-535, which is found in a domain of limited similarity to the active site serine of serine proteinases, to threonine.	./cache/cord-293375-qcy56ui7.txt	./txt/cord-293375-qcy56ui7.txt