id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-102570-lpwwlrqm	Fenn, Gareth D.	Crystallization and structure of ebselen bound to cysteine 141 of human inositol monophosphatase (IMPase)	2020-08-18		.txt	text/plain	3428	205	63	In the human-IMPase-complex ebselen, in a ring opened conformation, is covalently attached to Cys141, a residue located away from the active site. In the crystal structure presented in this publication, the active site in the tetramer is still accessible, suggesting that ebselen may function as an allosteric inhibitor, or may block the binding of partner proteins. Synopsis Here we present a 1.47Å crystal structure of human inositol monophosphatase (IMPase) bound to the inhibitor ebselen (PDB entry 6ZK0). In this paper, we present a 1.47Å structure of ebselen covalently bound to cysteine residue 141 of human IMPase (PDB entry 6ZK0). Each monomer of IMPase in this structure has a single ebselen molecule bound to Cys141 (PDB entry 6ZK0). The IMPase crystal structure that is presented (PDB entry 6ZK0) has ebselen covalently attached to Cys141, however it is not clear to what extent this binding brings about ebselen's inhibitory effects on IMPase.	./cache/cord-102570-lpwwlrqm.txt	./txt/cord-102570-lpwwlrqm.txt