West Nile Virus Core Protein: Tetramer Structure and Ribbon Formation

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 h...

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Bibliographic Details
Published in:Structure (London) 2004-07, Vol.12 (7), p.1157-1163
Main Authors: Dokland, Terje, Walsh, Martin, Mackenzie, Jason M., Khromykh, Alexander A., Ee, Kim-Huey, Wang, Sifang
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Crystallography, X-Ray
Molecular Sequence Data
Protein Structure, Quaternary
Protein Structure, Secondary
Viral Core Proteins - chemistry
West Nile virus
West Nile virus - chemistry
West Nile virus - metabolism
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Summary: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.
ISSN:0969-2126
1878-4186
DOI:10.1016/j.str.2004.04.024