The open pore conformation of potassium channels

Youxing Jiang, Alice Lee, Jiayun Chen, Martine Cadene, Brian T. Chait and Roderick MacKinnon ()
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Youxing Jiang: Rockefeller University
Alice Lee: Rockefeller University
Jiayun Chen: Rockefeller University
Martine Cadene: Rockefeller University
Brian T. Chait: Rockefeller University
Roderick MacKinnon: Rockefeller University

Nature, 2002, vol. 417, issue 6888, 523-526

Abstract: Abstract Living cells regulate the activity of their ion channels through a process known as gating. To open the pore, protein conformational changes must occur within a channel's membrane-spanning ion pathway. KcsA and MthK, closed and opened K+ channels, respectively, reveal how such gating transitions occur. Pore-lining ‘inner’ helices contain a ‘gating hinge’ that bends by approximately 30°. In a straight conformation four inner helices form a bundle, closing the pore near its intracellular surface. In a bent configuration the inner helices splay open creating a wide (12 Å) entryway. Amino-acid sequence conservation suggests a common structural basis for gating in a wide range of K+ channels, both ligand- and voltage-gated. The open conformation favours high conduction by compressing the membrane field to the selectivity filter, and also permits large organic cations and inactivation peptides to enter the pore from the intracellular solution.

Date: 2002
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DOI: 10.1038/417523a

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