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- W2044318670 abstract "Crystal structures of a genogroup II.4 human norovirus polymerase bound to an RNA primer–template duplex and the substrate analogue 2′-amino-2′-deoxycytidine-5′-triphosphate have been determined to 1.8 Å resolution. The alteration of the substrate-binding site that is required to accommodate the 2′-amino group leads to a rearrangement of the polymerase active site and a disruption of the coordination shells of the active-site metal ions. The mode of binding seen for 2′-amino-2′-deoxycytidine-5′-triphosphate suggests a novel molecular mechanism of inhibition that may be exploited for the design of inhibitors targeting viral RNA polymerases." @default.
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- W2044318670 date "2009-07-01" @default.
- W2044318670 modified "2023-09-27" @default.
- W2044318670 title "Binding of 2′-Amino-2′-Deoxycytidine-5′-Triphosphate to Norovirus Polymerase Induces Rearrangement of the Active Site" @default.
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- W2044318670 doi "https://doi.org/10.1016/j.jmb.2009.04.069" @default.
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