| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2052264 | FEBS Letters | 2005 | 4 Pages |
Abstract
Various neurotoxic peptides modulate voltage-gated sodium (NaV) channels and thereby affect cellular excitability. δ-Conotoxins from predatory cone snails slow down inactivation of NaV channels, but their interaction site and mechanism of channel modulation are unknown. Here, we show that δ-conotoxin SVIE from Conus striatus interacts with a conserved hydrophobic triad (YFV) in the domain-4 voltage sensor of NaV channels. This site overlaps with that of the scorpion α-toxin Lqh-2, but not with the α-like toxin Lqh-3 site. δ-SVIE functionally competes with Lqh-2, but exhibits strong cooperativity with Lqh-3, presumably by synergistically trapping the voltage sensor in its “on” position.
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Authors
Enrico Leipold, Alfred Hansel, Baldomero M. Olivera, Heinrich Terlau, Stefan H. Heinemann,