Cyclic nucleotide-gated channels: shedding light on the opening of a channel pore.

Autor: Flynn, Galen E., Johnson, J. P., Zagotta, William N., Flynn, G E, Johnson, J P Jr, Zagotta, W N
Předmět:
Zdroj: Nature Reviews Neuroscience; Sep2001, Vol. 2 Issue 9, p643-651, 9p, 4 Color Photographs, 5 Diagrams, 3 Graphs
Abstrakt: Few proteins have been described functionally in such detail as ion channels. All ion channels open and close their ion-conducting pores, a process referred to as gating. The recent crystallization of the P-loop-containing channel KcsA has cast channel function in a new light. Results relating to a variety of P-loop-containing channels are converging on a common mechanism in which separation of the inner helices that line the pore results in channel opening. At the same time, differences ? some subtle and some perhaps more profound ? have emerged between channel types. Here we highlight the evidence for a specific conformational change during the gating of cyclic nucleotide-gated channels, and compare and contrast this evidence to that obtained for other channels. [ABSTRACT FROM AUTHOR]
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