NADH quinone oxidoreductase (NQO1) with inhibitor dicoumarol
From Proteopedia
| Line 1: | Line 1: | ||
== The crystal structure of NQO1 in complex with its potent inhibitor dicoumarol == | == The crystal structure of NQO1 in complex with its potent inhibitor dicoumarol == | ||
| - | NAD(P)H quinone oxidoreductase 1 (NQO1) is a ubiquitous flavoenzyme that catalyzes two electron reduction of quinones to hydroquinones utilizing NAD(P)H as an electron donor. NQO1 binds and stabilizes several short-lived proteins including the tumor suppressors p53 and p73 and the enzyme ornithine decarboxylase (ODC). Dicoumarol is a widely used potent competitive inhibitor of NQO1 enzymatic activity, which competes with NAD(P)H for binding to NQO1. Dicoumarol also disrupts the binding of NQO1 to p53, p73 and ODC and induces their ubiquitin-independent proteasomal degradation. We report here the crystal structure of human NQO1 in complex with dicoumarol at | + | NAD(P)H quinone oxidoreductase 1 (NQO1) is a ubiquitous flavoenzyme that catalyzes two electron reduction of quinones to hydroquinones utilizing NAD(P)H as an electron donor. NQO1 binds and stabilizes several short-lived proteins including the tumor suppressors p53 and p73 and the enzyme ornithine decarboxylase ([[ODC]])[[hemoglobin]]. Dicoumarol is a widely used potent competitive inhibitor of NQO1 enzymatic activity, which competes with NAD(P)H for binding to NQO1. Dicoumarol also disrupts the binding of NQO1 to p53, p73 and ODC and induces their ubiquitin-independent proteasomal degradation. We report here the crystal structure of human NQO1 in complex with dicoumarol at |
[[Image:Figure1A copy.jpg|border|center|300px]] | [[Image:Figure1A copy.jpg|border|center|300px]] | ||
Revision as of 13:58, 21 October 2007
The crystal structure of NQO1 in complex with its potent inhibitor dicoumarol
NAD(P)H quinone oxidoreductase 1 (NQO1) is a ubiquitous flavoenzyme that catalyzes two electron reduction of quinones to hydroquinones utilizing NAD(P)H as an electron donor. NQO1 binds and stabilizes several short-lived proteins including the tumor suppressors p53 and p73 and the enzyme ornithine decarboxylase (ODC)hemoglobin. Dicoumarol is a widely used potent competitive inhibitor of NQO1 enzymatic activity, which competes with NAD(P)H for binding to NQO1. Dicoumarol also disrupts the binding of NQO1 to p53, p73 and ODC and induces their ubiquitin-independent proteasomal degradation. We report here the crystal structure of human NQO1 in complex with dicoumarol at
sna
Proteopedia Page Contributors and Editors (what is this?)
Alexander Berchansky, Orly Dym, Michal Harel, Jaime Prilusky, Moshe Ben-David, Joel L. Sussman, David Canner, Eric Martz
