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West Nile virus core protein; tetramer structure and ribbon formation
Authors:Dokland Terje  Walsh Martin  Mackenzie Jason M  Khromykh Alexander A  Ee Kim-Huey  Wang Sifang
Institution:Institute of Molecular and Cell Biology, Singapore, Republic of Singapore. dokland@uab.edu
Abstract: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 alpha helices and forms dimers that are organized into tetramers. The tetramers form extended filamentous ribbons resembling the stacked alpha helices seen in HEAT protein structures.
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