Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 390, Issue 1, Pages 10-16Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.04.069
Keywords
calicivirus; positive-strand RNA virus; viral replication; enzyme inhibitor; antiviral
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Funding
- Natural Sciences and Engineering Research Council of Canada [262089]
- Canadian Institutes of Health Research (CIHI) [MOP-67209]
- Spanish Ministerio de Educacion y Ciencia [B102006-00827]
- Fondo Europeo de Desarrollo Regional
- CIHR
- University of Saskatchewan
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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 angstrom 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. (C) 2009 Elsevier Ltd. All rights reserved.
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