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Originally published in Science Express on 7 July 2005
Science 5 August 2005:
Vol. 309. no. 5736, pp. 897 - 903
DOI: 10.1126/science.1116269
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Research Articles

Crystal Structure of a Mammalian Voltage-Dependent Shaker Family K+ Channel

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

Voltage-dependent potassium ion (K+) channels (Kv channels) conduct K+ ions across the cell membrane in response to changes in the membrane voltage, thereby regulating neuronal excitability by modulating the shape and frequency of action potentials. Here we report the crystal structure, at a resolution of 2.9 angstroms, of a mammalian Kv channel, Kv1.2, which is a member of the Shaker K+ channel family. This structure is in complex with an oxido-reductase ß subunit of the kind that can regulate mammalian Kv channels in their native cell environment. The activation gate of the pore is open. Large side portals communicate between the pore and the cytoplasm. Electrostatic properties of the side portals and positions of the T1 domain and ß subunit are consistent with electrophysiological studies of inactivation gating and with the possibility of K+ channel regulation by the ß subunit.

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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K. Moncoq, G. Kemp, X. Li, L. Fliegel, and H. S. Young (2008)
J. Biol. Chem. 283, 4145-4154
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Modification of K+ channel-drug interactions by ancillary subunits.
G. C. L. Bett and R. L. Rasmusson (2008)
J. Physiol. 586, 929-950
   Abstract »    Full Text »    PDF »
The Activation Gate and Gating Mechanism of the NMDA Receptor.
H.-R. Chang and C.-C. Kuo (2008)
J. Neurosci. 28, 1546-1556
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Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel.
G. M. Clayton, S. Altieri, L. Heginbotham, V. M. Unger, and J. H. Morais-Cabral (2008)
PNAS 105, 1511-1515
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Intrinsic Electrostatic Potential in the BK Channel Pore: Role in Determining Single Channel Conductance and Block.
I. Carvacho, W. Gonzalez, Y. P. Torres, S. Brauchi, O. Alvarez, F. D. Gonzalez-Nilo, and R. Latorre (2008)
J. Gen. Physiol. 131, 147-161
   Abstract »    Full Text »    PDF »


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