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...
मुख्य लेखकों: | De Colibus, L, Sonnen, A, Morris, K, Siebert, C, Abrusci, P, Plitzko, J, Hodnik, V, Leippe, M, Volpi, E, Anderluh, G, Gilbert, R |
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स्वरूप: | Journal article |
भाषा: | English |
प्रकाशित: |
2012
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समान संसाधन
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Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition
द्वारा: De Colibus, L, और अन्य
प्रकाशित: (2012) -
Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin.
द्वारा: Bakrac, B, और अन्य
प्रकाशित: (2008) -
Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin
द्वारा: Bakrač, B, और अन्य
प्रकाशित: (2008) -
Temporary Membrane Permeabilization via the Pore-Forming Toxin Lysenin
द्वारा: Nisha Shrestha, और अन्य
प्रकाशित: (2020-05-01) -
Insights into the Voltage Regulation Mechanism of the Pore-Forming Toxin Lysenin
द्वारा: Sheenah Lynn Bryant, और अन्य
प्रकाशित: (2018-08-01)