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J Biol Chem. 2012 Dec 14;287(51):43063-70. doi: 10.1074/jbc.M112.415091. Epub 2012 Oct 24.

Crystal structure of a voltage-gated K+ channel pore module in a closed state in lipid membranes.

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1
Section of Neurobiology, Division of Biological Sciences, University of California San Diego, La Jolla, California 92093, USA.

Erratum in

  • J Biol Chem. 2013 Feb 1;288(5):3476.

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 3.1 Å resolution 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.

PMID:
23095758
PMCID:
PMC3522301
DOI:
10.1074/jbc.M112.415091
[Indexed for MEDLINE]
Free PMC Article
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