id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-303692-py908dt8	Langley, Caroline	Structure of interferon-stimulated gene product 15 (ISG15) from the bat species Myotis davidii and the impact of interdomain ISG15 interactions on viral protein engagement	2019-01-01		.txt	text/plain	6198	316	55	title: Structure of interferon-stimulated gene product 15 (ISG15) from the bat species Myotis davidii and the impact of interdomain ISG15 interactions on viral protein engagement davidii ISG15, we use this protease as a biochemical tool; specifically, as a tool to illuminate the importance of the hydrophobic interdomain interface of ISG15 and how residue variation in this region between different species of ISG15s leads to biochemical differences in ISG15-protein engagement. With the exception of Pro38, which is a histidine residue in hISG15, all of these positions are conserved between bISG15 and the ISG15s from mice and humans. Taking the ITC data as a whole, the impact of mutations at Phe40 in bISG15 and its counterparts highlights the importance of ISG15 interdomain interactions in the effective binding of ISG15 by a protein that engages more than one domain of ISG15.	./cache/cord-303692-py908dt8.txt	./txt/cord-303692-py908dt8.txt