Structures of NS5 Methyltransferase from Zika Virus.
Coloma, J., Jain, R., Rajashankar, K.R., Garcia-Sastre, A., Aggarwal, A.K.(2016) Cell Rep 16: 3097-3102
- PubMed: 27633330 
- DOI: https://doi.org/10.1016/j.celrep.2016.08.091
- Primary Citation of Related Structures:  
5KQR, 5KQS - PubMed Abstract: 
The Zika virus (ZIKV) poses a major public health emergency. To aid in the development of antivirals, we present two high-resolution crystal structures of the ZIKV NS5 methyltransferase: one bound to S-adenosylmethionine (SAM) and the other bound to SAM and 7-methyl guanosine diphosphate (7-MeGpp). We identify features of ZIKV NS5 methyltransferase that lend to structure-based antiviral drug discovery. Specifically, SAM analogs with functionalities on the C¦Â atom of the methionine portion of the molecules that occupy the RNA binding tunnel may provide better specificity relative to human RNA methyltransferases.
Organizational Affiliation: 
Department of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.