English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/110349
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Citado 36 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar EndNote (RIS)Exportar EndNote (RIS)
Título

The coat protein of Rabbit hemorrhagic disease virus contains a molecular switch at the N-terminal region facing the inner surface of the capsid

Autor Bárcena, Juan; Verdaguer, Núria ; Roca, Ramón; Morales, Mónica; Angulo, Iván ; Risco, Cristina; Carrascosa, José L.; Torres, Juan María; Castón, José R.
Palabras clave VLP(s)
Virus-like particle(s)
Virus capsid
Three-dimensional structure
Three-dimensional reconstruction
RHDV
3DR
Cryo-electron microscopy
Cryo-EM
Molecular switch
Fecha de publicación 25-abr-2004
EditorAcademic Press
Citación Virology 322(1): 118-134 (2004)
ResumenTo function adequately, many if not all proteins involved in macromolecular assemblies show conformational polymorphism as an intrinsic feature. This general strategy has been described for many essential cellular processes. Here we describe this structural polymorphism in a viral protein, the coat protein of Rabbit hemorrhagic disease virus (RHDV), which is required during virus capsid assembly. By combining genetic, structure modeling, and cryo-electron microscopy and image processing analysis, we have established the mechanism that allows RHDV coat protein to switch among quasi-equivalent conformational states to achieve the appropriate curvature for the formation of a closed shell. The RHDV capsid structure is based on a T = 3 lattice, containing 180 copies of identical subunits, similar to those of other caliciviruses. The quasi-equivalent interactions between the coat proteins are achieved by the N-terminal region of a subset of subunits, which faces the inner surface of the capsid shell. Mutant coat protein lacking this N-terminal sequence assembles into T = 1 capsids. Our results suggest that the polymorphism of the RHDV T = 3 capsid might bear resemblance to that of plant virus T = 3 capsids. © 2004 Elsevier Inc. All rights reserved.
Versión del editorhttp://dx.doi.org/10.1016/j.virol.2004.01.021
URI http://hdl.handle.net/10261/110349
DOI10.1016/j.virol.2004.01.021
Identificadoresdoi: 10.1016/j.virol.2004.01.021
issn: 0042-6822
Aparece en las colecciones: (CNB) Artículos
(IBMB) Artículos
(CID) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 



NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.