A Twist on Potassium Channel Gating

A Twist on Potassium Channel Gating

The selectivity filter of potassium channels, the narrowest segment of the pore, permits only potassium ions to diffuse through the pore. Clarke et al. (2010) now present 11 structures of an inwardly rectifying potassium channel, providing evidence that the selectivity filter functions in channel gating and conformational changes in the cytoplasmic domains correlate with pore opening.

Channel gating: Twist to open

Recent studies of the bacterial mechanosensitive channel MscL have combined a number of different approaches to come up with a model for the channel gating mechanism.

Ion-Channel Gating: Twist to open

Three-dimensional images of the open state of the nicotinic acetylcholine receptor have been obtained at 9 A resolution. Comparison with the closed state reveals the structural basis of channel gating.

hERG potassium channel inhibition by ivabradine requires channel gating.

Lipid-dependent gating of a voltage-gated potassium channel

Recent studies hypothesized that phospholipids stabilize two voltage-sensing arginine residues of certain voltage-gated potassium channels in activated conformations. It remains unclear how lipids directly affect these channels. Here, by examining the conformations of the KvAP in different lipids, we showed that without voltage change, the voltage-sensor domains switched from the activated to t...