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On the stability of parainfluenza virus 5 F proteins.
Poor, Taylor A; Song, Albert S; Welch, Brett D; Kors, Christopher A; Jardetzky, Theodore S; Lamb, Robert A.
Afiliación
  • Poor TA; Department of Molecular Biosciences Northwestern University, Evanston, Illinois, USA.
  • Song AS; Department of Molecular Biosciences Northwestern University, Evanston, Illinois, USA.
  • Welch BD; Department of Molecular Biosciences Northwestern University, Evanston, Illinois, USA Howard Hughes Medical Institute, Northwestern University, Evanston, Illinois, USA.
  • Kors CA; Department of Molecular Biosciences Northwestern University, Evanston, Illinois, USA Howard Hughes Medical Institute, Northwestern University, Evanston, Illinois, USA.
  • Jardetzky TS; Department of Structural Biology, Stanford University, Stanford, California, USA.
  • Lamb RA; Department of Molecular Biosciences Northwestern University, Evanston, Illinois, USA Howard Hughes Medical Institute, Northwestern University, Evanston, Illinois, USA ralamb@northwestern.edu.
J Virol ; 89(6): 3438-41, 2015 Mar.
Article en En | MEDLINE | ID: mdl-25589638
The crystal structure of the F protein (prefusion form) of the paramyxovirus parainfluenza virus 5 (PIV5) WR isolate was determined. We investigated the basis by which point mutations affect fusion in PIV5 isolates W3A and WR, which differ by two residues in the F ectodomain. The P22 stabilizing site acts through a local conformational change and a hydrophobic pocket interaction, whereas the S443 destabilizing site appears sensitive to both conformational effects and amino acid charge/polarity changes.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Virales de Fusión / Virus de la Parainfluenza 5 Límite: Humans Idioma: En Revista: J Virol Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Virales de Fusión / Virus de la Parainfluenza 5 Límite: Humans Idioma: En Revista: J Virol Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos