Extended surface for membrane association in Zika virus NS1 structure

被引：125

作者：

Brown, W. Clay ^{[1
]}

Akey, David L. ^{[1
]}

Konwerski, Jamie R. ^{[1
]}

Tarrasch, Jeffrey T. ^{[1
]}

Skiniotis, Georgios ^{[1
,2
]}

Kuhn, Richard J. ^{[3
,4
]}

Smith, Janet L. ^{[1
,2
]}

机构：

[1] Univ Michigan, Inst Life Sci, Ann Arbor, MI 48109 USA

[2] Univ Michigan, Dept Biol Chem, Ann Arbor, MI 48109 USA

[3] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA

[4] Purdue Univ, Purdue Inst Inflammat Immunol & Infect Dis, W Lafayette, IN 47907 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2016年 / 23卷 / 09期

关键词：

D O I：

10.1038/nsmb.3268

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Zika virus, which has been implicated in an increase in neonatal microcephaly and Guillain-Barre 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.

引用

页码：865 / 867

页数：3

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