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Nat Struct Mol Biol. 2016 Sep;23(9):865-7. doi: 10.1038/nsmb.3268. Epub 2016 Jul 25.

Extended surface for membrane association in Zika virus NS1 structure.

Author information

1
Life Sciences Institute, University of Michigan, Ann Arbor, Michigan, USA.
2
Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA.
3
Department of Biological Sciences, Purdue University, West Lafayette, Indiana, USA.
4
Purdue Institute for Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, Indiana, USA.

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.

PMID:
27455458
PMCID:
PMC5951387
DOI:
10.1038/nsmb.3268
[Indexed for MEDLINE]
Free PMC Article

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