March 1, 1999The Journal of General PhysiologyOpen Access

Helical Structure and Packing Orientation of the S2 Segment in the Shaker K+ Channel

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Population

Xenopus oocytes expressing Shaker K+ channel mutants

Design

Preclinical

Authors

SMStephen A. MonksHoward Hughes Medical Institute DNDaniel NeedlemanHarvard University CMChristopher MillerBrigham and Women's Hospital

Discussion

Member takes

Implication

Refines voltage-gated K+ channel models; extends helix-packing hypotheses but leaves open mammalian validation.

Structured PICO

Population

Xenopus oocytes expressing Shaker K+ channel mutants

Intervention

Single tryptophan (or alanine for native tryptophan) mutations in the S2 segment

Outcome

Voltage-dependent K+ currents and channel gating propertiessurrogate

The S2 segment of the Shaker K+ channel forms a transmembrane alpha helix with distinct faces for lipid interaction and packing against other segments.

Cite This Study

Monks et al. (1999) studied this question.

synapsesocial.com/papers/6a82619870df46ce3ea214a2 https://doi.org/10.1085/jgp.113.3.415

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Helical Structure and Packing Orientation of the S2 Segment in the Shaker K+ Channel

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Helical Structure and Packing Orientation of the S2 Segment in the Shaker K+ Channel

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider