| Literature DB >> 27455458 |
W Clay Brown1, David L Akey1, Jamie R Konwerski1, Jeffrey T Tarrasch1, Georgios Skiniotis1,2, Richard J Kuhn3,4, Janet L Smith1,2.
Abstract
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.Entities:
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Year: 2016 PMID: 27455458 PMCID: PMC5951387 DOI: 10.1038/nsmb.3268
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN: 1545-9985 Impact factor: 15.369