3h5y

Publication Abstract from PubMed

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 A 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.

Binding of 2'-amino-2'-deoxycytidine-5'-triphosphate to norovirus polymerase induces rearrangement of the active site.,Zamyatkin DF, Parra F, Machin A, Grochulski P, Ng KK J Mol Biol. 2009 Jul 3;390(1):10-6. Epub 2009 May 5. PMID:19426741^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.