The open pore conformation of potassium channels

Youxing Jiang, Alice Lee, Jiayun Chen, Martine Cadene, Brian T. Chait, Roderick MacKinnon

Research output: Contribution to journalArticle

1018 Scopus citations

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 (12Å) 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.

Original languageEnglish (US)
Pages (from-to)523-526
Number of pages4
JournalNature
Volume417
Issue number6888
DOIs
StatePublished - May 30 2002

ASJC Scopus subject areas

  • General

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    Jiang, Y., Lee, A., Chen, J., Cadene, M., Chait, B. T., & MacKinnon, R. (2002). The open pore conformation of potassium channels. Nature, 417(6888), 523-526. https://doi.org/10.1038/417523a