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Elucidating the Structural Basis of the Intracellular pH Sensing Mechanism of TASK-2 K(2)P Channels

Two-pore domain potassium (K(2)P) channels maintain the cell’s background conductance by stabilizing the resting membrane potential. They assemble as dimers possessing four transmembrane helices in each subunit. K(2)P channels were crystallized in “up” and “down” states. The movements of the pore-li...

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Detalles Bibliográficos
Autores principales:	Bustos, Daniel, Bedoya, Mauricio, Ramírez, David, Concha, Guierdy, Zúñiga, Leandro, Decher, Niels, Hernández-Rodríguez, Erix W., Sepúlveda, Francisco V., Martínez, Leandro, González, Wendy
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2020
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7013731/ https://www.ncbi.nlm.nih.gov/pubmed/31947679 http://dx.doi.org/10.3390/ijms21020532

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Correction: Concha, G., et al. The Insensitivity of TASK-3 K(2)P Channels to External Tetraethylammonium (TEA) Partially Depends on the Cap Structure. Int. J. Mol. Sci. 2018, 19, 2437
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