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December 22, 2014eLifeOpen Access

Domain–domain interactions determine the gating, permeation, pharmacology, and subunit modulation of the IKs ion channel

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Authors

MZMark A. ZaydmanWashington University in St. Louis MKMarina A. KasimovaNovo Nordisk (Denmark)KMKelli McFarlandWashington University in St. Louis

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Implication

May refine IKs gating models; leaves open clinical translation for LQTS or arrhythmia therapies.

Key Points

Key points are not available for this paper at this time.

Cite This Study

Zaydman et al. (2014) studied this question.

synapsesocial.com/papers/6a7154db5d37378ac1de7d15 https://doi.org/10.7554/elife.03606

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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1Biology of the KCNQ1 Potassium Channel2014 · 101 citations
2I <sub>Ks</sub> channels open slowly because KCNE1 accessory subunits slow the movement of S4 voltage sensors in KCNQ1 pore-forming subunits2013 · 58 citations
3Regulation of Voltage-Activated K+ Channel Gating by Transmembrane β Subunits2012 · 51 citations
4KCNQ1 and KCNE1 in the IKs Channel Complex Make State-dependent Contacts in their Extracellular Domains2008 · 82 citations
5Voltage‐dependent inactivation of the human K<sup>+</sup> channel KvLQT1 is eliminated by association with minimal K<sup>+</sup> channel (minK) subunits1998 · 163 citations