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- W3201845440 abstract "The viral protease domain (NS3pro) of dengue virus is essential for virus replication, and its cofactor NS2B is indispensable for the proteolytic function. Although several NS3pro-NS2B complex structures have been obtained, the dynamic property of the complex remains poorly understood. Using NMR relaxation techniques, here we found that NS3pro-NS2B exists in both closed and open conformations that are in dynamic equilibrium on a submillisecond timescale in aqueous solution. Our structural information indicates that the C-terminal region of NS2B is disordered in the minor open conformation but folded in the major closed conformation. Using mutagenesis, we showed that the closed-open conformational equilibrium can be shifted by changing NS2B stability. Moreover, we revealed that the proteolytic activity of NS3pro-NS2B correlates well with the population of the closed conformation. Our results suggest that the closed-open conformational equilibrium can be used by both nature and humanity to control the replication of dengue virus." @default.
- W3201845440 created "2021-10-11" @default.
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- W3201845440 date "2021-06-01" @default.
- W3201845440 modified "2023-10-18" @default.
- W3201845440 title "Dengue virus protease activity modulated by dynamics of protease cofactor" @default.
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- W3201845440 doi "https://doi.org/10.1016/j.bpj.2021.04.015" @default.
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