Extended surface for membrane association in Zika virus NS1 structure.
Extended surface for membrane association in Zika virus NS1 structure.
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DOI:
10.1038/nsmb.3268
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发表时间:
2016-09
影响因子:
16.8
通讯作者:
Smith JL
中科院分区:
文献类型:
--
作者:
Brown WC;Akey DL;Konwerski JR;Tarrasch JT;Skiniotis G;Kuhn RJ;Smith JL
The Zika virus, which is 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.
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