Selected article for: "active site and drug target"
Author: Mateo, Roberto; Nagamine, Claude M.; Kirkegaard, Karla
Title: Suppression of Drug Resistance in Dengue Virus
  • Document date: 2015_12_15
    • ID: 6bx2nrui_23
    Snippet: It is intriguing that the two mutations conferring MK-0608 resistance identified in this work mapped to the methyltransferase domain of NS5 (Fig. 3D) . The methyltransferase and polymerase domains are known to interact functionally and structurally (16, 26) . Thus, it is possible either that the A60T and Y201H mutations exert allosteric effects on the polymerase active site or that MK-0608 inhibits methyltransferase activity directly. Whatever th.....
    Document: It is intriguing that the two mutations conferring MK-0608 resistance identified in this work mapped to the methyltransferase domain of NS5 (Fig. 3D) . The methyltransferase and polymerase domains are known to interact functionally and structurally (16, 26) . Thus, it is possible either that the A60T and Y201H mutations exert allosteric effects on the polymerase active site or that MK-0608 inhibits methyltransferase activity directly. Whatever the particular step of RNA synthesis inhibited by MK-0608, it does not appear to be a dominant drug target. It is possible that other aspects of NS5 function, such as RNA binding, elongation, or translocation, will be targets (27) .

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