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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2018
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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. |
format | Online Article Text |
id | pubmed-9083029 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
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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