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 Cβ atom of the methionine portion of the molecules that occupy the RNA binding tunnel may provide better specificity relative to human RNA methyltransferases.
journal_name
Cell Repjournal_title
Cell reportsauthors
Coloma J,Jain R,Rajashankar KR,García-Sastre A,Aggarwal AKdoi
10.1016/j.celrep.2016.08.091subject
Has Abstractpub_date
2016-09-20 00:00:00pages
3097-3102issue
12issn
2211-1247pii
S2211-1247(16)31200-1journal_volume
16pub_type
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