Cargando…
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...
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: | |
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 |
Ejemplares similares
-
Crystallographic characterization of CCG repeats
por: Kiliszek, Agnieszka, et al.
Publicado: (2012) -
Structure of the SARS coronavirus main proteinase as an active C(2) crystallographic dimer
por: Xu, Ting, et al.
Publicado: (2005) -
A Transient Homotypic Interaction Model for the Influenza A Virus NS1 Protein Effector Domain
por: Kerry, Philip S., et al.
Publicado: (2011) -
A crystallographic and modelling study of a human telomeric RNA (TERRA) quadruplex
por: Collie, Gavin W., et al.
Publicado: (2010) -
Crystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A
por: Kaminishi, Tatsuya, et al.
Publicado: (2015)