Structural highlights
Publication Abstract from PubMed
An outbreak of Zika virus (ZIKV) infection has been reported in South and Central America and the Caribbean. Neonatal microcephaly potentially associated with ZIKV infection has already caused a public health emergency of international concern. Currently, there are no clinically effective vaccines or antiviral drugs available to treat ZIKV infection. The methyltransferase domain (MTase) of ZIKV nonstructural protein 5 (NS5) can sequentially methylate guanine N-7 and ribose 2'-O to form m7NGpppA2'Om cap structure in the new RNA transcripts. This methylation step is crucial for ZIKV replication cycle and evading the host immune system, making it a target for drug design. Here, we present the 1.76 A crystal structure of ZIKV MTase in complex with the byproduct SAH, providing insight into the elegant methylation process, which will benefit the following antiviral drug development.
The conformational changes of Zika virus methyltransferase upon converting SAM to SAH.,Zhou H, Wang F, Wang H, Chen C, Zhang T, Han X, Wang D, Chen C, Wu C, Xie W, Wang Z, Zhang L, Wang L, Yang H Oncotarget. 2017 Feb 28;8(9):14830-14834. doi: 10.18632/oncotarget.14780. PMID:28122329[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhou H, Wang F, Wang H, Chen C, Zhang T, Han X, Wang D, Chen C, Wu C, Xie W, Wang Z, Zhang L, Wang L, Yang H. The conformational changes of Zika virus methyltransferase upon converting SAM to SAH. Oncotarget. 2017 Feb 28;8(9):14830-14834. doi: 10.18632/oncotarget.14780. PMID:28122329 doi:http://dx.doi.org/10.18632/oncotarget.14780
