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NMR analysis of the dynamic exchange of the NS2B cofactor between open and closed conformations of the West Nile Virus NS2B-NS3 protease

Su, Xun-Cheng; Ozawa, Kiyoshi; Qi, Ruhu; Vasudevan, Subhash G.; Lim, Siew P.; Otting, Gottfried


BACKGROUND The two-component NS2B-NS3 proteases of West Nile and dengue viruses are essential for viral replication and established targets for drug development. In all crystal structures of the proteases to date, the NS2B cofactor is located far from the substrate binding site (open conformation) in the absence of inhibitor and lining the substrate binding site (closed conformation) in the presence of an inhibitor. METHODS In this work, nuclear magnetic resonance (NMR) spectroscopy of isotope...[Show more]

CollectionsANU Research Publications
Date published: 2009-12-08
Type: Journal article
Source: PLoS Neglected Tropical Diseases
DOI: 10.1371/journal.pntd.0000561


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