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...
Príomhchruthaitheoirí: | 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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Formáid: | Journal article |
Teanga: | English |
Foilsithe / Cruthaithe: |
2012
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Míreanna comhchosúla
Míreanna comhchosúla
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Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition
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