Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition.

Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition.

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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...

Disgrifiad llawn

Manylion Llyfryddiaeth
Prif Awduron:	De Colibus, L, Sonnen, A, Morris, K, Siebert, C, Abrusci, P, Plitzko, J, Hodnik, V, Leippe, M, Volpi, E, Anderluh, G, Gilbert, R
Fformat:	Journal article
Iaith:	English
Cyhoeddwyd:	2012

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