December 21, 2017Pflügers Archiv - European Journal of PhysiologyOpen Access

Gating mechanism of Kv11.1 (hERG) K+ channels without covalent connection between voltage sensor and pore domains

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Population

Kv11.1 (hERG, KCNH2) voltage-gated potassium channels

Comparison

Progressive displacement of the split position… vs Intact channels or channels with different split…

Design

Preclinical

Authors

PPPilar de la PeñaUniversidad de Oviedo PDPedro Domı́nguezUniversidad de Oviedo FBFrancisco BarrosUniversidad de Oviedo

Discussion

Member takes

Implication

Challenges classical Kv11.1 activation models; leaves open translational relevance to human cardiac arrhythmias.

Structured PICO

Population

Kv11.1 (hERG, KCNH2) voltage-gated potassium channels

Intervention

Progressive displacement of the split position (non-covalent connection) from the end to the beginning of the S4-S5 linker

Comparator

Intact channels or channels with different split positions

Outcome

Voltage-dependent gating properties (activation voltage dependence, z g value, ΔG 0, activation time course, deactivation)surrogate

Alterations in the covalent connection between the voltage sensor and pore domains impact structural reorganizations of the voltage sensor domain in Kv11.1 channels, challenging classical views of channel activation.

Cite This Study

Peña et al. (2017) studied this question.

synapsesocial.com/papers/6a83eeb0a3cef8348e997a1f https://doi.org/10.1007/s00424-017-2093-9

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Gating mechanism of Kv11.1 (hERG) K+ channels without covalent connection between voltage sensor and pore domains

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Gating mechanism of Kv11.1 (hERG) K+ channels without covalent connection between voltage sensor and pore domains

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider