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==Dengue Virus inside Cell==<StructureSection load='1ok8' size='500' side='right' caption='Dengue virus inside cell (PDB entry [[1ok8]])' scene=''>Anything in this section will appear adjacent to the 3D structure and will be scrollable.</StructureSection>
==Dengue Virus inside Cell==<StructureSection load='1ok8' size='500' side='right' caption='Dengue virus inside cell (PDB entry [[1ok8]])' scene=''>Anything in this section will appear adjacent to the 3D structure and will be scrollable.</StructureSection>


==GTP to Methyltransferase==<StructureSection load='2j7w' size='500' side='right' caption='NS5 polymerase (PDB entry [[2j7w]])' scene=''>The N-terminal domain has the capacity to bind GTP, hold the guanosine of the viral cap structure, and synthesize two different methylation reactions that are required for the formation of the RNA cap (3). A GTP-binding site in the N-terminal domain is suggested to be a cap-binding site for the Dengue-2-methyltransferase (4). The C-terminal subdomain is an RNA-dependent-RNA polymerase (RdRp) domain. The core subunit is responsible for Ado-Met binding and catalytic activity due to the GTP-binding pocket (3).<scene name='56/565763/Active_site_gtp/1'>GTP in active site</scene>.</StructureSection>
Dengue NS3 Protein<StructureSection load='2j7w' size='500' side='right' caption='NS5 polymerase (PDB entry [[2j7w]])' scene=''>The N-terminal domain has the capacity to bind GTP, hold the guanosine of the viral cap structure, and synthesize two different methylation reactions that are required for the formation of the RNA cap (3). A GTP-binding site in the N-terminal domain is suggested to be a cap-binding site for the Dengue-2-methyltransferase (4). The C-terminal subdomain is an RNA-dependent-RNA polymerase (RdRp) domain. The core subunit is responsible for Ado-Met binding and catalytic activity due to the GTP-binding pocket (3).<scene name='56/565763/Active_site_gtp/1'>GTP in active site</scene><scene name='56/565763/Sah/1'>NS5</scene></StructureSection>


==Dengue Methyltransferase==<StructureSection load='1l9k' size='500' side='right' caption='NS5 methyltransferase (PDB entry [[1l9k]])' scene=''>Dengue-2 NS5 methyltransferase is one of the seven nonstructural proteins in the polyprotein encoded by the flavivirus genome's single open reading frame. This is the non-structural protein, NS5, which is the largest and most conserved protein in a flavivirus.The Dengue-2-virus methyltransferase has an N-terminal subdomain, a core subdomain, a C-terminal subdomain (3) and a K-D-K-E motif (9). Dengue-2 NS5 methyltransferase also has an "S-adenosyl methionine-dependent methyltransferase fold" structure which is essentially a "sandwich" of αβα sheets in the N-terminal domain<scene name='56/565763/Sah/1'>NS5</scene></StructureSection>
Dengue NS5 Protein<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.  
 
 
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.  
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>
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>


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Sunjeet Virdi