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Comment
. 2018 Jun 20:12:174.
doi: 10.3389/fncel.2018.00174. eCollection 2018.

Commentary: A channelopathy mutation in the voltage-sensor discloses contributions of a conserved phenylalanine to gating properties of Kv1.1 channels and ataxia

Sonia Hasan  1 , Therese Hunter  2 , Gary Hunter  2 , Mauro Pessia  2   3 , Maria Cristina D'Adamo  2
Affiliations
Comment

Commentary: A channelopathy mutation in the voltage-sensor discloses contributions of a conserved phenylalanine to gating properties of Kv1.1 channels and ataxia

Sonia Hasan et al. Front Cell Neurosci. .
No abstract available

Keywords: KV1.1; channelopathy; hydrophobic gating; potassium channels; shaker-related; voltage-gated.

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Figures

Figure 1
Figure 1
(A) The full model of the Kv1.1 potassium channel based on Kv1.2 coordinates is shown in the open state with subunits colored gray, green, blue, and cyan. (B) Enlargement of the section boxed in (A) with functional helices colored (S5, blue, is from a different subunit and labeled B). Residues involved in voltage sensing are drawn and labeled with those involved in the hydrophobic interactions between subunits. (C,D) The S4 helix and S5 helix of subunit (B) in the wild-type and F303V mutant, respectively. Interatomic distances are shown as dashed lines with distances shown in Å. A slight discrepancy in distances may apply due to the mobile nature of the S4 segment. The figure was drawn using The PyMOL (Molecular Graphics System, Version 2.0 Schrödinger, LLC), and adapted from Hasan et al. (2017).
See this image and copyright information in PMC

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References

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