Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
Pore-forming toxins act by forming oligomeric pores in lipid membranes. Here the authors report the crystal structure of the lysenin pore, providing insights into the assembly and function of the pore in addition to suggesting that its properties make lysenin potentially well-suited for nanopore sen...
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| Autores principales: | , , , , , , , , , , , , , , , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2016
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/f5376f82acc44644923125077c3a3c57 |
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| Sumario: | Pore-forming toxins act by forming oligomeric pores in lipid membranes. Here the authors report the crystal structure of the lysenin pore, providing insights into the assembly and function of the pore in addition to suggesting that its properties make lysenin potentially well-suited for nanopore sensing applications. |
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