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

Abstract:

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 against parasites by attacking their membranes to form pores. SM has important roles in cell membranes and lysenin is a popular SM-labeling reagent. The structure of lysenin suggests common ancestry wi...

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Publisher copy:
10.1016/j.str.2012.06.011

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Journal:
Structure
Volume:
20
Issue:
9
Pages:
1498-1507
Publication date:
2012-09-05
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:c1cab8c3-f7b5-4b5f-a78f-9e539b78dd31
Source identifiers:
350831
Local pid:
pubs:350831
Language:
English

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