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Crystal Structure of a Voltage-gated K+ Channel Pore Module in a Closed State in Lipid Membranes.

Authors :
Santos, Jose S.
Asmar-Rovira, Guillermo A.
Gye Won Han
Wei Liu
Syeda, Ruhma
Cherezov, Vadim
Baker, Kent A.
Stevens, Raymond C.
Montal, Mauricio
Source :
Journal of Biological Chemistry. 12/14/2012, Vol. 287 Issue 51, p43063-43070. 8p.
Publication Year :
2012

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 3.1Å 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00219258
Volume :
287
Issue :
51
Database :
Academic Search Index
Journal :
Journal of Biological Chemistry
Publication Type :
Academic Journal
Accession number :
84505953
Full Text :
https://doi.org/10.1074/jbc.M112.415091