Structural highlights
Function
Q70ET3_9CALI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
See Also
References
- ↑ Zamyatkin DF, Parra F, Machin A, Grochulski P, Ng KK. Binding of 2'-amino-2'-deoxycytidine-5'-triphosphate to norovirus polymerase induces rearrangement of the active site. J Mol Biol. 2009 Jul 3;390(1):10-6. Epub 2009 May 5. PMID:19426741 doi:10.1016/j.jmb.2009.04.069
