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| Crystal structure of a mammalian voltage-dependent Shaker family K+ channel |
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| Author(s): Long SB, Campbell EB, MacKinnon R |
| Source: SCIENCE Volume: 309 Issue: 5736 Pages: 897-903 Published: AUG 5 2005 |
| Times Cited: 627 References: 54 |
| Abstract: Voltage-de pendent 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 etectrophysiologicat studies of inactivation gating and with the possibility of K+ channel regulation by the beta subunit. |
| Document Type: Article |
| Language: English |
| Reprint Address: MacKinnon, R (reprint author), Rockefeller Univ, Howard Hughes Med Inst, Lab Mol Neurobiol & Biophys, 1230 York Ave, New York, NY 10021 USA |
Addresses:
1. Rockefeller Univ, Howard Hughes Med Inst, Lab Mol Neurobiol & Biophys, New York, NY 10021 USA |
| Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: 953SS |
| ISSN: 0036-8075 |
| DOI: 10.1126/science.1116269 |
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