Binding of 2'-amino-2'-deoxycytidine-5'-triphosphate to norovirus polymerase induces rearrangement of the active site.

@article{Zamyatkin2009BindingO2,
  title={Binding of 2'-amino-2'-deoxycytidine-5'-triphosphate to norovirus polymerase induces rearrangement of the active site.},
  author={Dmitry F. Zamyatkin and Francisco Vargas Parra and Angeles Mach{\'i}n and Pawel Grochulski and Kenneth K S Ng},
  journal={Journal of molecular biology},
  year={2009},
  volume={390 1},
  pages={
          10-6
        }
}
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… CONTINUE READING
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