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. 2020 Jan 24;10:1572. doi: 10.3389/fphar.2019.01572

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Copyright © 2020 Butler, Helliwell, Zhang, Hancox and Dempsey

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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A “tryptophan clamp” connects the hERG turret helix with the top of the S5 helix. This motif that includes an interaction with F617 on the hERG pore helix is conserved throughout the KCNH family of channels that includes ERG, EAG and ELK variants, despite considerable sequence diversity in the turret helix itself (G584-I593 in hERG1). Helix interactions involving a cluster of aromatic side chains at the extracytoplasmic ends of S1, S5 and the pore helix may serve to anchor the VS domain against the pore as observed in other K_v channels (Lee et al., 2009); dEAG1 is drosophila EAG1; h, human.