Conservation of a crystallographic interface suggests a role for β-sheet augmentation in influenza virus NS1 multifunctionality

The effector domain (ED) of the influenza virus virulence factor NS1 is capable of interaction with a variety of cellular and viral targets, although regulation of these events is poorly understood. Introduction of a W187A mutation into the ED abolishes dimer formation; however, strand–strand intera...

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Detalles Bibliográficos
Autores principales: Kerry, Philip S., Long, Elizabeth, Taylor, Margaret A., Russell, Rupert J. M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2011
Materias:
Structural Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3151114/
https://www.ncbi.nlm.nih.gov/pubmed/21821881
http://dx.doi.org/10.1107/S1744309111019312

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3151114/
https://www.ncbi.nlm.nih.gov/pubmed/21821881
http://dx.doi.org/10.1107/S1744309111019312

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