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Review
. 2002 Oct;120(4):475-81.
doi: 10.1085/jgp.20028657.

The search is on for the voltage sensor-to-gate coupling

H Peter Larsson  1
Affiliations
Review

The search is on for the voltage sensor-to-gate coupling

H Peter Larsson. J Gen Physiol. 2002 Oct.
No abstract available

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Figures

F<sc>igure</sc> 1.
Figure 1.
Model of a voltage-activated ion channel. Cartoon of a Kv channel (only three out of the four subunits are shown) in the closed state (A) and the open state (B). S5, S6, and the S5-S6 loop (the P loop) from all four subunits contribute to the pore-forming domain. S1-S4 from each subunit form a voltage-sensing domain. S4 charges move outwards in response to a depolarization, triggering the opening of the activation gate (located at the bundle crossing at the COOH-terminal end of S6). The S4-S5 loop is here suggested as the coupling mechanism between S4 movement and the opening of the activation gate.
F<sc>igure</sc> 2.
Figure 2.
Opening and closing of the activation gate in bacterial K+ channels. Molecular models of the KcsA K+ channel (A) and the MthK K+ channel (B) (Doyle et al., 1998; Jiang et al., 2002a). Only two of four subunits are shown for simplicity. The larger circles are K+ ions, and the smaller, darker circle is a water molecule. The KcsA channel is presumably in a closed state, and the MthK channel is in an open state. The difference between the two structures suggests that bending of the M2 transmembrane segment opens K+ channels (Jiang et al., 2002b).
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