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:
影响因子:
--
通讯作者:
Wang S
中科院分区:
文献类型:
--
作者:
Dokland T;Walsh M;Mackenzie JM;Khromykh AA;Ee KH;Wang S
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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