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Published Online July 7, 2005
Science DOI: 10.1126/science.1116269

Research Articles

Submitted on June 17, 2005
Accepted on July 5, 2005

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

Stephen B. Long 1, Ernest B. Campbell 1, Roderick MacKinnon 1*

1 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.
Roderick MacKinnon , E-mail: mackinn{at}rockefeller.edu

Voltage-dependent K+ (Kv) channels conduct K+ ions across the cell membrane in response to changes in the membrane voltage, and thereby regulate neuronal excitability by modulating the shape and frequency of action potentials. Here we report the crystal structure at a resolution of 2.9 Å of a mammalian Kv channel, Kv1.2, a member of the Shaker K+ channel family. This structure is in complex with an oxido-reductase {beta} 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 {beta} subunit are consistent with electrophysiological studies of inactivation gating and with the possibility of K+ channel regulation by the {beta} subunit.


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