id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-280881-5o38ihe0	Wlodawer, Alexander	A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases	2003-11-11		.txt	text/plain	4862	220	51	These structures defined a novel family of enzymes, now called sedolisins or serine-carboxyl peptidases, that is characterized by the utilization of a fully conserved catalytic triad (Ser, Glu, Asp) and by the presence of an Asp in the oxyanion hole [8] . We have now applied the tools of molecular homology modeling to predicting a structure of CLN2 that could be used as a basis for a search for the biological substrates of this family of enzymes and for the design of specific inhibitors. Mammalian enzymes homologous to human CLN2 [2, 4] form a subfamily of sedolisins with highly conserved sequences ( Figure 1 ). Exploiting the sequence similarity between CLN2, sedolisin, and kumamolisin ( Figure 4 ), we have now used the experimentally obtained structures of the latter two enzymes to form a new, homology-derived model of human CLN2.	./cache/cord-280881-5o38ihe0.txt	./txt/cord-280881-5o38ihe0.txt