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...
المؤلفون الرئيسيون: | 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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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2012
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مواد مشابهة
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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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Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin.
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Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin
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