Dengue protease activity: The structural integrity and interaction of NS2B with NS3 protease and its potential as a drug target

Please use this identifier to cite or link to this item: https://doi.org/10.1042/BSR20100142

Title:	Dengue protease activity: The structural integrity and interaction of NS2B with NS3 protease and its potential as a drug target
Authors:	Phong, W.Y. Moreland, N.J. Lim, S.P. Wen, D. Paradkar, P.N. Vasudevan, S.G.
Keywords:	Allosteric inhibitor Dengue Flavivirus NS2B NS3 Protease
Issue Date:	Oct-2011
Citation:	Phong, W.Y., Moreland, N.J., Lim, S.P., Wen, D., Paradkar, P.N., Vasudevan, S.G. (2011-10). Dengue protease activity: The structural integrity and interaction of NS2B with NS3 protease and its potential as a drug target. Bioscience Reports 31 (5) : 399-409. ScholarBank@NUS Repository. https://doi.org/10.1042/BSR20100142
Abstract:	Flaviviral NS3 serine proteases require the NS2B cofactor region (cNS2B) to be active. Recent crystal structures of WNV (West Nile virus) protease in complex with inhibitors revealed that cNS2B participates in the formation of the protease active site. No crystal structures of ternary complexes are currently available for DENV (dengue virus) to validate the role of cNS2B in active site formation. In the present study, a GST (glutathione transferase) fusion protein of DENV-2 cNS2B 49-95 was used as a bait to pull down DENV-2 protease domain (NS3pro). The affinity of NS3pro for cNS2B was strong (equilibrium-binding constant
Source Title:	Bioscience Reports
URI:	http://scholarbank.nus.edu.sg/handle/10635/110517
ISSN:	01448463
DOI:	10.1042/BSR20100142
Appears in Collections:	Staff Publications

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