Pore-forming segments in voltage-gated chloride channels

C. Fahike, H. T. Yu, C. L. Beck, T. H. Rhodes, Jr George A.L.

Research output: Contribution to journalArticlepeer-review

151 Scopus citations

Abstract

The ability to differentiate between ions is a property of ion channels that is crucial for their biological functions. However, the fundamental structural features that define argon selectivity and distinguish anion- permeable from cation-permeable channels are poorly understood. Voltage- gated chloride (Cl-) channels belonging to the ClC family are ubiquitous and have been predicted to play important roles in many diverse physiological and pathophysiological processes. We have identified regions of a human skeletal muscle ClC isoform that contribute to formation of its anion-selective conduction pathway. A core structural element (P1 region) of the ClC channel pore spans an accessibility barrier between the internal and external milieu, and contains an evolutionarily conserved sequence motif: GKxGPxxH. Neighbouring sequences in the third and fifth transmembrane segments also contribute to isoform-specific differences in anion selectivity. The conserved motif in the Cl- channel P1 region may constitute a 'signature' sequence for an anion-selective ion pore by analogy with the homologous GYG sequence that is essential for selectivity in voltage-gated potassium ion (K+) channel pores.

Original languageEnglish (US)
Pages (from-to)529-532
Number of pages4
JournalNature
Volume390
Issue number6659
DOIs
StatePublished - Dec 1 1997

ASJC Scopus subject areas

  • General

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