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Article

A side chain in S6 influences both open-state stability and ion permeation in a voltage-gated K+ channel.

Pflugers Archiv : European journal of physiology - 1 Apr 1998

Liu Y, Joho R H

Abstract excerpt

Conservative substitutions of the conserved cysteine 393 (Cys393) in S6 of the voltage-gated K+ channel Kv2.1 predictably alter the stability of the open state and the conductances for K+ and Rb+. The polarity of the side chain at position 393 determines the stability of the open state, probably...

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Source

Identifiers

PMID: 9479018
DOI: 10.1007/s004240050566

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-9479018-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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A side chain in S6 influences both open-state stability and ion permeation in a voltage-gated K+ channel.PMID 9479018Read ↗

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A novel mechanism for fine-tuning open-state stability in a voltage-gated potassium channel.Semantic proximity Read ↗

Gating of shaker-type channels requires the flexibility of S6 caused by prolines.Semantic proximity Read ↗

Conformational dynamics of the inner pore helix of voltage-gated potassium channels.Semantic proximity Read ↗

Hydrophobic substitution mutations in the S4 sequence alter voltage-dependent gating in Shaker K+ channels.Semantic proximity Read ↗

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