Abstract
Voltage-gated K+ channels underlie the electrical excitability of cells. Each subunit of the functional tetramer consists of the tandem fusion of two modules, an N-terminal voltage-sensor and a C-terminal pore. To investigate how sensor coupling to the pore generates voltage-dependent channel opening, we solved the crystal structure and characterized the function of a voltage-gated K+ channel pore in a lipid membrane. The structure of a functional channel in a membrane environment at 3.1Åresolution establishes an unprecedented connection between channel structure and function. The structure is unique in delineating an ion-occupied ready to conduct selectivity filter, a confined aqueous cavity, and a closed activation gate, embodying a dynamic entity trapped in an unstable closed state.
Original language | English (US) |
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Pages (from-to) | 43063-43070 |
Number of pages | 8 |
Journal | Journal of Biological Chemistry |
Volume | 287 |
Issue number | 51 |
DOIs | |
State | Published - Dec 14 2012 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology