AutoriRojko N.; Dalla Serra M.; MacEk P.; Anderluh G.
AbstractActinoporins (APs) from sea anemones are ~ 20 kDa pore forming toxins with a ?-sandwich structure flanked by two ?-helices. The molecular mechanism of APs pore formation is composed of several well-defined steps. APs bind to membrane by interfacial binding site composed of several aromatic amino acid residues that allow binding to phosphatidylcholine and specific recognition of sphingomyelin. Subsequently, the N-terminal ?-helix from the ?-sandwich has to be inserted into the lipid/water interphase in order to form a functional pore. Functional studies and single molecule imaging revealed that only several monomers, 3-4, oligomerise to form a functional pore. In this model the ?-helices and surrounding lipid molecules build toroidal pore. In agreement, AP pores are transient and electrically heterogeneous. On the contrary, crystallized oligomers of actinoporin fragaceatoxin C were found to be composed of eight monomers with no lipids present between the adjacent ?-helices. This article is part of a Special Issue entitled: Pore-Forming Toxins edited by Maur Dalla Serra and Franco Gambale.
RivistaBiochimica Et Biophysica Acta. Biomembranes
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Pagina inizio446
Pagina fine456
Linee di Ricerca IBFMD.P01.028.001