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  • A novel mechanism of pore formation: membrane permeabilization by the N-terminal amphipathic region of equinatoxin
    Malovrh, Petra ...
    Equinatoxin II is a representatlve ot actinoporins, eukaryotic pore-forming toxins from sea anemones. It creates pares in natural and artifficial lipid membranes by an association of three or four ... monomers. Cysteinescanaing mutagenesis was used to study the structure of the N terminus, which is proposed to be crucial in transmembrane pore formation. We provide data for two steps of pore formation: a lipid-bound monomeric intermediate state and a flnal oligomeric pore. Results show that residues 10-28 are organized as an alpha-helix in both steps. In the first step, the whole region is transferred to a lipid-water interface, laying flat on the membrane. In the pore-forming state, the hydrophilic side of the amphipathic helix lines the pore lumen. Thepore has a restriction around Asp-10, according to the permeabilization ratio of ions flowing through pores formed by chemically modified mutants. A general model was introduced to derive the tilt angle of the helix from the ion current data. This study reveals that actinoporins use a unique single helix insertion mechanism for pore formation.
    Vir: The Journal of biological chemistry. - ISSN 0021-9258 (Letn. 278, št. 25, 2003, str. 22678-22685)
    Vrsta gradiva - članek, sestavni del
    Leto - 2003
    Jezik - angleški
    COBISS.SI-ID - 16160473

vir: The Journal of biological chemistry. - ISSN 0021-9258 (Letn. 278, št. 25, 2003, str. 22678-22685)
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