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1.D.40 The Protein-induced Lipid Toroidal Pore (Lipid Pore) Family

Stoddart et al. 2014 provided evidence for membrane proteins that stabilize lipid pores, probably as toroidal structures. They examined mutants of the staphylococcal α-hemolysin pore so severely truncated that the protein could not span a bilayer. The doughnut-like structures elicited well-defined transmembrane ionic currents by inducing pore formation in the underlying lipids. The formation of lipid pores, produced by a structurally defined protein, is supported by the lipid and voltage dependences of pore formation, and by molecular dynamics simulations. The role of stabilized lipid pores in amyloid disease, the action of antimicrobial peptides, and the assembly of the membrane- attack complexes of the immune system were discussed (Stoddart et al. 2014).

References associated with 1.D.40 family:

Stoddart D., Ayub M., Hofler L., Raychaudhuri P., Klingelhoefer JW., Maglia G., Heron A. and Bayley H. (2014). Functional truncated membrane pores. Proc Natl Acad Sci U S A. 111(7):2425-30. 24469792