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

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...

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Detalles Bibliográficos
Autores principales: Navarro-Retamal, Carlos, Caballero, Julio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9083029/
https://www.ncbi.nlm.nih.gov/pubmed/35541058
http://dx.doi.org/10.1039/c8ra04159h
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author Navarro-Retamal, Carlos
Caballero, Julio
author_facet Navarro-Retamal, Carlos
Caballero, Julio
author_sort Navarro-Retamal, Carlos
collection PubMed
description 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.
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spelling pubmed-90830292022-05-09 Energetic differences between non-domain-swapped and domain-swapped chain connectivities in the K2P potassium channel TRAAK Navarro-Retamal, Carlos Caballero, Julio RSC Adv Chemistry 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. The Royal Society of Chemistry 2018-07-25 /pmc/articles/PMC9083029/ /pubmed/35541058 http://dx.doi.org/10.1039/c8ra04159h Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Navarro-Retamal, Carlos
Caballero, Julio
Energetic differences between non-domain-swapped and domain-swapped chain connectivities in the K2P potassium channel TRAAK
title Energetic differences between non-domain-swapped and domain-swapped chain connectivities in the K2P potassium channel TRAAK
title_full Energetic differences between non-domain-swapped and domain-swapped chain connectivities in the K2P potassium channel TRAAK
title_fullStr Energetic differences between non-domain-swapped and domain-swapped chain connectivities in the K2P potassium channel TRAAK
title_full_unstemmed Energetic differences between non-domain-swapped and domain-swapped chain connectivities in the K2P potassium channel TRAAK
title_short Energetic differences between non-domain-swapped and domain-swapped chain connectivities in the K2P potassium channel TRAAK
title_sort energetic differences between non-domain-swapped and domain-swapped chain connectivities in the k2p potassium channel traak
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9083029/
https://www.ncbi.nlm.nih.gov/pubmed/35541058
http://dx.doi.org/10.1039/c8ra04159h
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