title: West Nile virus core protein; tetramer structure and ribbon formation.
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.
authors.affiliation: Institute of Molecular and Cell Biology, Singapore, Republic of Singapore. dokland@uab.edu
authors.forename: Terje
authors.initials: T
authors.lastname: Dokland
authors.forename: Martin
authors.initials: M
authors.lastname: Walsh
authors.forename: Jason M
authors.initials: JM
authors.lastname: Mackenzie
authors.forename: Alexander A
authors.initials: AA
authors.lastname: Khromykh
authors.forename: Kim-Huey
authors.initials: KH
authors.lastname: Ee
authors.forename: Sifang
authors.initials: S
authors.lastname: Wang
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D014758:Viral Core Proteins / Q000737:chemistry*; D014902:West Nile virus / Q000737:chemistry* / Q000378:metabolism
chemical_list: D014758:Viral Core Proteins