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Extended surface for membrane association in Zika virus NS1 structure
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Journal Article
Extended surface for membrane association in Zika virus NS1 structure
2016
Overview
The crystal structure of full-length NS1 protein from Zika virus reveals an extended surface for membrane association and a highly variable polar surface.
The Zika virus, which has been implicated in an increase in neonatal microcephaly and Guillain–Barré syndrome, has spread rapidly through tropical regions of the world. The virulence protein NS1 functions in genome replication and host immune-system modulation. Here, we report the crystal structure of full-length Zika virus NS1, revealing an elongated hydrophobic surface for membrane association and a polar surface that varies substantially among flaviviruses.
Publisher
Nature Publishing Group US,Nature Publishing Group
