Deciphering the molecular basis for nucleotide selection by the West Nile virus RNA helicase.

ABSTRACT: The West Nile virus RNA helicase uses the energy derived from the hydrolysis of nucleotides to separate complementary strands of RNA. Although this enzyme has a preference for ATP, the bias towards this purine nucleotide cannot be explained on the basis of specific protein-ATP interactions. Moreover, the enzyme does not harbor the characteristic Q-motif found in other helicases that regulates binding to ATP. In the present study, we used structural homology modeling to generate a model of the West Nile virus RNA helicase active site that provides instructive findings on the interaction between specific amino acids and the ATP substrate. In addition, we evaluated both the phosphohydrolysis and the inhibitory potential of a collection of 30 synthetic purine analogs. A structure-guided alanin

SUBMITTER: Despins S 

PROVIDER: S-EPMC2938200 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature