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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Veröffentlicht in:Structure (London) 2004-07, Vol.12 (7), p.1157-1163
Hauptverfasser: Dokland, Terje, Walsh, Martin, Mackenzie, Jason M., Khromykh, Alexander A., Ee, Kim-Huey, Wang, Sifang
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Sprache:eng
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Zusammenfassung: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