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Article

The neutral, hydrophobic isoleucine at position I521 in the extracellular S4 domain of hERG contributes to channel gating equilibrium.

American journal of physiology. Cell physiology - 15 Aug 2013

Dou Ying, Goodchild Samuel J, Velde Robert Vander, Wu Yue, Fedida David

Abstract excerpt

The human ether-a-go-go related (hERG) potassium channel has unusual functional characteristics in that the rates of channel activation and deactivation are much slower than inactivation, which is attributed to specific structural elements within the NH2 terminus and the S1-S4 voltage-sensing domains (VSD). Although the charged residues in the VSD have been extensively modified and mutated as a result, the role...

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PMID: 23761630
DOI: 10.1152/ajpcell.00147.2013

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The neutral, hydrophobic isoleucine at position I521 in the extracellular S4 domain of hERG contributes to channel gating equilibrium.PMID 23761630Read ↗

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Cooperative interactions between R531 and acidic residues in the voltage sensing module of hERG1 channels.Semantic proximity Read ↗

Fast and slow voltage sensor movements in HERG potassium channels.Semantic proximity Read ↗

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Voltage sensor movement in the hERG K+ channel.Semantic proximity Read ↗

The hERG K(+) channel S4 domain L532P mutation: characterization at 37°C.Semantic proximity Read ↗

The evolutionarily conserved residue A653 plays a key role in HERG channel closing.Semantic proximity Read ↗

The voltage-sensing domain of a hERG1 mutant is a cation-selective channel.Semantic proximity Read ↗

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The pore domain outer helix contributes to both activation and inactivation of the HERG K+ channel.Semantic proximity Read ↗

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