Crystal structure of a mammalian voltage-dependent Shaker family K+ channel.
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 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.
Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Stephen B
SB
Long
Ernest B
EB
Campbell
Roderick
R
Mackinnon
D000818:Animals; D020134:Catalytic Domain; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004563:Electrochemistry; D051663:Kv1.2 Potassium Channel; D008958:Models, Molecular; D010843:Pichia; D011188:Potassium / Q000737:chemistry; D024642:Potassium Channels, Voltage-Gated / Q000737:chemistry*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry
C496972:Kcna2 protein, rat; D051663:Kv1.2 Potassium Channel; D024642:Potassium Channels, Voltage-Gated; D021122:Protein Subunits; D011994:Recombinant Proteins; D011188:Potassium