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Hydrophobic interactions between the S5 segment and the pore helix stabilizes the closed state of Slo2.1 potassium channels
Under normal physiological conditions, Slo2.1 K(+) channels are in a closed state unless activated by an elevation in [Na(+)](i). Fenamates such as niflumic acid also activate Slo2.1. Previous studies suggest that activation of Slo2.1 channels is mediated by a conformational change in the selectivit...
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| Publicado no: | Biochim Biophys Acta |
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| Principais autores: | , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2015
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4779660/ https://ncbi.nlm.nih.gov/pubmed/26724206 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bbamem.2015.12.024 |
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