The presence of the iron-sulfur motif is important for the conformational stability of the antiviral protein, Viperin.
Viperin, an antiviral protein, has been shown to contain a CX(3)CX(2)C motif, which is conserved in the radical S-adenosyl-methionine (SAM) enzyme family. A triple mutant which replaces these three cysteines with alanines has been shown to have severe deficiency in antiviral activity. Since the crys...
Guardado en:
Autores principales: | Shubhasis Haldar, Simantasarani Paul, Nidhi Joshi, Anindya Dasgupta, Krishnananda Chattopadhyay |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2012
|
Materias: | |
Acceso en línea: | https://doaj.org/article/2fc1e933accd4621b36c3839bd4a3813 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Viperin is an important host restriction factor in control of Zika virus infection
por: Kylie H. Van der Hoek, et al.
Publicado: (2017) -
SUMO-interacting motifs of human TRIM5α are important for antiviral activity.
por: Gloria Arriagada, et al.
Publicado: (2011) -
Constraint-based modeling of yeast mitochondria reveals the dynamics of protein import and iron-sulfur cluster biogenesis
por: Carl Malina, et al.
Publicado: (2021) -
Probing the influence of mutations on FUS condensates, one molecule at a time
por: Krishnananda Chattopadhyay
Publicado: (2021) -
Structure of the respiratory MBS complex reveals iron-sulfur cluster catalyzed sulfane sulfur reduction in ancient life
por: Hongjun Yu, et al.
Publicado: (2020)