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Issue 47, 2018, Issue in Progress
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Energetic differences between non-domain-swapped and domain-swapped chain connectivities in the K2P potassium channel TRAAK

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Abstract

Two-pore domain (K2P) channels are twofold symmetric K+ channels which control cell excitability by enabling the leak of potassium ions from cells in response to physicochemical stimuli. Crystallization of K2P channels revealed the presence of several structural features, which include an external cap. In the available crystallographic structures, the cap is present as non-domain-swapped (NDS) and domain-swapped (DS) chain conformations, where DS chain conformation exchanges two opposing outer helices 180° around the channel. In this work, energy differences between the residues located at the highest point of the cap in NDS and DS conformations were evaluated for TRAAK, a K2P channel that was crystallized in both conformations. Results indicated a preference for DS conformation, but this result is not extensible to TASK K2P channels.

Graphical abstract: Energetic differences between non-domain-swapped and domain-swapped chain connectivities in the K2P potassium channel TRAAK

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Supplementary files

Article information


Submitted
16 May 2018
Accepted
19 Jul 2018
First published
25 Jul 2018

This article is Open Access

RSC Adv., 2018,8, 26610-26618
Article type
Paper

Energetic differences between non-domain-swapped and domain-swapped chain connectivities in the K2P potassium channel TRAAK

C. Navarro-Retamal and J. Caballero, RSC Adv., 2018, 8, 26610
DOI: 10.1039/C8RA04159H

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