August 1, 1998The Journal of General PhysiologyOpen Access

A Mutation in S6 of Shaker Potassium Channels Decreases the K+ Affinity of an Ion Binding Site Revealing Ion–Ion Interactions in the Pore

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Population

Shaker potassium channels

Comparison

A463C mutation in the S6 segment vs Wild-type Shaker potassium channels

Design

Preclinical

Authors

EOE OgielskaUniversity of California, Berkeley RARichard W. AldrichElectrophysiology

Discussion

Member takes

Implication

Does not inform clinical ion channel management; extends model-system understanding of dual Na/K pore occupancy but leaves relevance to cardiac channels open.

Structured PICO

Population

Shaker potassium channels

Intervention

A463C mutation in the S6 segment

Comparator

Wild-type Shaker potassium channels

Outcome

Apparent internal potassium affinity of the channel poresurrogate

The A463C mutation in the Shaker potassium channel decreases potassium affinity, revealing that sodium and potassium can simultaneously occupy the pore and interact.

Cite This Study

Ogielska et al. (1998) studied this question.

synapsesocial.com/papers/6a835ed7dfd29b4838caa1b3 https://doi.org/10.1085/jgp.112.2.243

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Implication

Does not inform clinical ion channel management; extends model-system understanding of dual Na/K pore occupancy but leaves relevance to cardiac channels open.

A Mutation in S6 of Shaker Potassium Channels Decreases the K+ Affinity of an Ion Binding Site Revealing Ion–Ion Interactions in the Pore

Discussion

Member takes

Implication

Structured PICO

Cite This Study

A Mutation in S6 of Shaker Potassium Channels Decreases the K+ Affinity of an Ion Binding Site Revealing Ion–Ion Interactions in the Pore

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider