Sandbox 1k4r: Difference between revisions

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==Dengue Protease and Helicase==<StructureSection load='2vbc' size='500' side='right' caption='Structure of protease and helicase (PDB entry [[2vbc]])' scene=''>The NS2B cofactor is critical for proteolytic activation of the flavivirus NS3 protease. To elucidate the
Dengue Protease and Helicase<StructureSection load='2vbc' size='500' side='right' caption='Structure of protease and helicase (PDB entry [[2vbc]])' scene=''>The NS3 protease is a serine protease that can also function as a RNA helicase and RTPase/NTPase. The enzymatic function of this protease is important for the Dengue virus to replicate. This enzyme of the virus is also a potential target for vaccines and antiviral drugs.  
mechanism involved in NS2B-mediated activation of NS3 protease, molecular dynamic simulation, principal
The catalytic triad (His-51, Asp-75 and Ser-135), is found between these two β-barrels, and its activity is dependent on the presence of the <scene name='56/565763/Ns2b/2'>NS2B</scene>. This cofactor wraps around the NS3 protease domain and becomes part of the active site. The NS2B cofactor is critical for proteolytic activation of the NS3 protease. The NS3 protease is made up of an extensive network of hydrogen bond and hydrophobic interaction, making it very rigid. NS2B is also important in contributing to substrate binding. This implies that the NS2B cofactor acts as an enzyme activator as well as being directly involved in substrate binding/interactions.</StructureSection>
component analysis, molecular docking, mutagenesis, and bioassay studies were carried out on both the dengue
virus NS3pro and NS2B-NS3pro systems. <scene name='56/565763/Ns2b/2'>NS2B</scene>.</StructureSection>