期刊
CELL REPORTS
卷 16, 期 12, 页码 3097-3102出版社
CELL PRESS
DOI: 10.1016/j.celrep.2016.08.091
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资金
- National Institute of General Medical Sciences (NIGMS) from the NIH [P41 GM103403]
- National Cancer Institute [ACB-12002]
- NIGMS [AGM-12006]
- NIH-ORIP HEI grant [S10 RR029205]
- DOE Office of Science by Argonne National Laboratory [DE-AC02-06CH11357]
- NIH [U19AI118610]
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 Cb atom of the methionine portion of the molecules that occupy the RNA binding tunnel may provide better specificity relative to human RNA methyltransferases.
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