Abstract
The structure of a complex containing a toxin bound to a potassium ion channel has been solved for the first time, revealing how scorpions have designed toxins that can recognize and target the filter that controls the movement of potassium ions through these channels.
Highlights
Scorpion toxins that block protein pores hold a special place in the annals of ion channel biophysics and writing in eLife, Rod MacKinnon and colleagues at Rockefeller University—including Anirban Banerjee as first author—report that they have used X-ray crystallography to determine the structure of charybdotoxin, a scorpion toxin, bound to the pore of a voltage-dependent potassium ion (Kv) channel (Figure 1A; Banerjee et al, 2013)
The story begins at Brandeis University back in the 1980s, when Chris Miller and colleagues discovered that the venom of the Israeli scorpion, Leiurus quinquestriatus, contained a small protein that bound to a single site on the external end of a BK channel—BK is short for ‘big potassium’, and a BK channel is a particular type of Kv channel that allows a large current of potassium ions to pass through it (Miller et al, 1985)
The one-to-one stoichiometry between charybdotoxin and the channel hinted that the toxin targeted the pore because it was assumed at the time that Kv channels are formed by four identical subunits and that the pore would be located at the interface between them
Summary
Scorpion toxins that block protein pores hold a special place in the annals of ion channel biophysics and writing in eLife, Rod MacKinnon and colleagues at Rockefeller University—including Anirban Banerjee as first author—report that they have used X-ray crystallography to determine the structure of charybdotoxin, a scorpion toxin, bound to the pore of a voltage-dependent potassium ion (Kv) channel (Figure 1A; Banerjee et al, 2013). Ion channels | The scorpion toxin and the potassium channel of the toxin depended on the concentration of potassium ions on the inside of the cell membrane (MacKinnon and Miller, 1988).
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