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Originally published in Science Express on 7 July 2005
Science 5 August 2005:
Vol. 309. no. 5736, pp. 903 - 908
DOI: 10.1126/science.1116270
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Research Articles

Voltage Sensor of Kv1.2: Structural Basis of Electromechanical Coupling

Stephen B. Long, Ernest B. Campbell, Roderick MacKinnon*

Voltage-dependent ion channels contain voltage sensors that allow them to switch between nonconductive and conductive states over the narrow range of a few hundredths of a volt. We investigated the mechanism by which these channels sense cell membrane voltage by determining the x-ray crystal structure of a mammalian Shaker family potassium ion (K+) channel. The voltage-dependent K+ channel Kv1.2 grew three-dimensional crystals, with an internal arrangement that left the voltage sensors in an apparently native conformation, allowing us to reach three important conclusions. First, the voltage sensors are essentially independent domains inside the membrane. Second, they perform mechanical work on the pore through the S4-S5 linker helices, which are positioned to constrict or dilate the S6 inner helices of the pore. Third, in the open conformation, two of the four conserved Arg residues on S4 are on a lipid-facing surface and two are buried in the voltage sensor. The structure offers a simple picture of how membrane voltage influences the open probability of the channel.

Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.

* To whom correspondence should be addressed. E-mail: mackinn{at}rockefeller.edu

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Relationship between Pore Occupancy and Gating in BK Potassium Channels.
R. A. Piskorowski and R. W. Aldrich (2006)
J. Gen. Physiol. 127, 557-576
   Abstract »    Full Text »    PDF »
Interaction of d-Tubocurarine with Potassium Channels: Molecular Modeling and Ligand Binding.
A. Rossokhin, G. Teodorescu, S. Grissmer, and B. S. Zhorov (2006)
Mol. Pharmacol. 69, 1356-1365
   Abstract »    Full Text »    PDF »
Voltage-dependent Gating Rearrangements in the Intracellular T1-T1 Interface of a K+ Channel.
G. Wang and M. Covarrubias (2006)
J. Gen. Physiol. 127, 391-400
   Abstract »    Full Text »    PDF »
1,4-Diazabicyclo[2.2.2]octane Derivatives: A Novel Class of Voltage-Gated Potassium Channel Blockers.
E. Gordon, J.-L. Cohen, R. Engel, and G. W. Abbott (2006)
Mol. Pharmacol. 69, 718-726
   Abstract »    Full Text »    PDF »
Role of Charged Residues in the S1-S4 Voltage Sensor of BK Channels.
Z. Ma, X. J. Lou, and F. T. Horrigan (2006)
J. Gen. Physiol. 127, 309-328
   Abstract »    Full Text »    PDF »
OLD PORE - NEW EDITION.
H. Merzendorfer (2006)
J. Exp. Biol. 209, iii
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Identification by mass spectrometry and functional characterization of two phosphorylation sites of KCNQ2/KCNQ3 channels.
T. S. Surti, L. Huang, Y. N. Jan, L. Y. Jan, and E. C. Cooper (2005)
PNAS 102, 17828-17833
   Abstract »    Full Text »    PDF »
Overview of Molecular Relationships in the Voltage-Gated Ion Channel Superfamily.
F. H. Yu, V. Yarov-Yarovoy, G. A. Gutman, and W. A. Catterall (2005)
Pharmacol. Rev. 57, 387-395
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Tryptophan scanning mutagenesis of the HERG K+ channel: the S4 domain is loosely packed and likely to be lipid exposed.
R. N. Subbiah, M. Kondo, T. J. Campbell, and J. I. Vandenberg (2005)
J. Physiol. 569, 367-379
   Abstract »    Full Text »    PDF »


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