Structural highlights
Publication Abstract from PubMed
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 Cbeta atom of the methionine portion of the molecules that occupy the RNA binding tunnel may provide better specificity relative to human RNA methyltransferases.
Structures of NS5 Methyltransferase from Zika Virus.,Coloma J, Jain R, Rajashankar KR, Garcia-Sastre A, Aggarwal AK Cell Rep. 2016 Sep 20;16(12):3097-102. doi: 10.1016/j.celrep.2016.08.091. Epub, 2016 Sep 12. PMID:27633330[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Coloma J, Jain R, Rajashankar KR, Garcia-Sastre A, Aggarwal AK. Structures of NS5 Methyltransferase from Zika Virus. Cell Rep. 2016 Sep 20;16(12):3097-102. doi: 10.1016/j.celrep.2016.08.091. Epub, 2016 Sep 12. PMID:27633330 doi:http://dx.doi.org/10.1016/j.celrep.2016.08.091
