September 11, 1998FEBS Letters

Probing pore topology and conformational changes of Kir2.1 potassium channels by cysteine scanning mutagenesis

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Population

Kir2.1 potassium channels (inward rectifier K+ channel) with mutant C149F background

Design

Preclinical

Authors

YKYoshihiro KuboElectrophysiology YMYoshimichi MurataNational Institute of Advanced Industrial Science and Technology SHStefan H. HeinemannElectrophysiology

Discussion

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Implication

Indicates external Kir2.1 H5 pore accessibility without state-dependent shifts; extends channel models but leaves open human cardiac relevance.

Structured PICO

Population

Kir2.1 potassium channels (inward rectifier K+ channel) with mutant C149F background

Intervention

Cysteine (Cys) scanning mutagenesis (introduction of Cys residues at 10 positions in the H5 pore region) and application of Cys-modifying reagents

Outcome

Changes in current amplitude and speed of channel modification upon application of Cys-specific reagentssurrogate

The H5 pore region of Kir2.1 channels faces externally and does not undergo state-dependent conformational changes, contrasting with voltage-gated K+ channels.

Cite This Study

Kubo et al. (1998) studied this question.

synapsesocial.com/papers/6a851fd7f14ace264a43cffd https://doi.org/10.1016/s0014-5793(98)01038-2

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Implication

Indicates external Kir2.1 H5 pore accessibility without state-dependent shifts; extends channel models but leaves open human cardiac relevance.

Probing pore topology and conformational changes of Kir2.1 potassium channels by cysteine scanning mutagenesis

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Probing pore topology and conformational changes of Kir2.1 potassium channels by cysteine scanning mutagenesis

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider