Dengue protease activity: The structural integrity and interaction of NS2B with NS3 protease and its potential as a drug target
Phong, W.Y. Moreland, N.J. Lim, S.P. Wen, D. Paradkar, P.N. Vasudevan, S.G.
Phong, W.Y.
Moreland, N.J.
Lim, S.P.
Wen, D.
Paradkar, P.N.
Citations
Altmetric:
Alternative Title
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
Keywords
Allosteric inhibitor, Dengue, Flavivirus, NS2B, NS3, Protease
Source Title
Bioscience Reports
Publisher
Series/Report No.
Collections
Rights
Date
2011-10
DOI
10.1042/BSR20100142
Type
Article