Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition.
Pore-forming proteins insert from solution into membranes to create lesions, undergoing a structural rearrangement often accompanied by oligomerization. Lysenin, a pore-forming toxin from the earthworm Eisenia fetida, specifically interacts with sphingomyelin (SM) and may confer innate immunity agai...
Principais autores: | De Colibus, L, Sonnen, A, Morris, K, Siebert, C, Abrusci, P, Plitzko, J, Hodnik, V, Leippe, M, Volpi, E, Anderluh, G, Gilbert, R |
---|---|
Formato: | Journal article |
Idioma: | English |
Publicado em: |
2012
|
Registros relacionados
-
Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition
por: De Colibus, L, et al.
Publicado em: (2012) -
Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin.
por: Bakrac, B, et al.
Publicado em: (2008) -
Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin
por: Bakrač, B, et al.
Publicado em: (2008) -
Temporary Membrane Permeabilization via the Pore-Forming Toxin Lysenin
por: Nisha Shrestha, et al.
Publicado em: (2020-05-01) -
Insights into the Voltage Regulation Mechanism of the Pore-Forming Toxin Lysenin
por: Sheenah Lynn Bryant, et al.
Publicado em: (2018-08-01)