Faculty Opinions recommendation of Crystal structure of full-length Zika virus NS5 protein reveals a conformation similar to Japanese encephalitis virus NS5.
Year: 2017
Type: peer-review
Abstract: The rapid spread of the recent Zika virus (ZIKV) epidemic across various countries in the American continent poses a major health hazard for the unborn fetuses of pregnant women.To date, there is no effective medical intervention.The nonstructural protein 5 of Zika virus (ZIKV-NS5) is critical for ZIKV replication through the 5 0 -RNA capping and RNA polymerase activities present in its N-terminal methyltransferase (MTase) and C-terminal RNA-dependent RNA polymerase (RdRp) domains, respectively.The crystal structure of the full-length ZIKV-NS5 protein has been determined at 3.05 A ˚resolution from a crystal belonging to space group P2 1 2 1 2 and containing two protein molecules in the asymmetric unit.The structure is similar to that reported for the NS5 protein from Japanese encephalitis virus and suggests opportunities for structure-based drug design targeting either its MTase or RdRp domain.
Authors: Zucai Suo, Andrew Reed
Institutions: Florida State University, The Ohio State University
Language: English
Field: Medicine
Domain: Health Sciences
Open Access status: green
OpenAlex ID: W4239223154