Development of a S-adenosylmethionine analog that intrudes the RNA-cap binding site of Zika methyltransferase

Rinku Jain, Kyle V. Butler, Javier Coloma, Jian Jin, Aneel K. Aggarwal

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

The Zika virus (ZIKV) has emerged as a major health hazard. We present here a high resolution structure (1.55 Å) of ZIKV NS5 methyltransferase bound to a novel S-adenosylmethionine (SAM) analog in which a 4-fluorophenyl moiety substitutes for the methyl group. We show that the 4-fluorophenyl moiety extends into a portion of the RNA binding tunnel that typically contains the adenosine 2′OH of the RNA-cap moiety. Together, the new SAM analog and the high-resolution crystal structure are a step towards the development of antivirals against ZIKV and other flaviviruses.

Original languageEnglish
Article number1632
JournalScientific Reports
Volume7
Issue number1
DOIs
StatePublished - 1 Dec 2017

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