Sandbox 1k4r: Difference between revisions
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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> | ||
== | ==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 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 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 | ||
mechanism involved in NS2B-mediated activation of NS3 protease, molecular dynamic simulation, principal | |||
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> | |||