West nile virus core protein: Tetramer structure and ribbon formation
Contribuinte(s) |
Victoria Mountain Andrej Sali Christopher Lima and Joseph Puglisi |
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Data(s) |
01/01/2004
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Resumo |
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 a. 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. |
Identificador | |
Idioma(s) |
eng |
Publicador |
Cell Press |
Palavras-Chave | #West Nile Virus #Structure #Assembly #Encephalitis #Biochemistry & Molecular Biology #Biophysics #Cell Biology #Tick-borne Encephalitis #Electron-density Maps #Dengue Virus #Capsid Protein #Envelope Glycoprotein #Flavivirus Kunjin #Crystal-structure #Organization #Maturation #Particles #C1 #270303 Virology #730101 Infectious diseases |
Tipo |
Journal Article |