West Nile virus core protein; tetramer structure and ribbon formation.

West Nile virus core protein; tetramer structure and ribbon formation.
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DOI:
10.1016/j.str.2004.04.024
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发表时间:
2004-07
期刊:
Structure (London, England : 1993)
影响因子:
--
通讯作者:
Wang S
Wang S
中科院分区:
其他
文献类型:
--
作者:
Dokland T;Walsh M;Mackenzie JM;Khromykh AA;Ee KH;Wang S

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我们确定了西尼罗病毒 (WNV) Kunjin 亚型核心 (C) 蛋白的晶体结构,该亚型与 WNV NY99 株密切相关,目前是美国的主要健康威胁。WNV 是有包膜 RNA 病毒黄病毒科的成员,含有许多重要的人类病原体。 C蛋白与RNA基因组相关,并形成被病毒颗粒的包膜包围的内部核心。 C 蛋白结构包含四个 α 螺旋,形成二聚体,再组织成四聚体。四聚体形成延伸的丝状带,类似于 HEAT 蛋白质结构中看到的堆叠 α 螺旋。
We have determined the crystal structure of the core (C) protein from the Kunjin subtype of West Nile virus (WNV), closely related to the NY99 strain of WNV, currently a major health threat in the U.S. WNV is a member of the Flaviviridae family of enveloped RNA viruses that contains many important human pathogens. The C protein is associated with the RNA genome and forms the internal core which is surrounded by the envelope in the virion. The C protein structure contains four α helices and forms dimers that are organized into tetramers. The tetramers form extended filamentous ribbons resembling the stacked α helices seen in HEAT protein structures.
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