West nile virus core protein: Tetramer structure and ribbon formation


Autoria(s): Dokland, T.; Walsh, M.; Mackenzie, J. M.; Khromykh, A. A.; Ee, K. H.; Wang, S. F.
Contribuinte(s)

Victoria Mountain

Andrej Sali

Christopher Lima and Joseph Puglisi

Data(s)

01/01/2004

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

http://espace.library.uq.edu.au/view/UQ:69842

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