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Tethered peptide neurotoxins display two blocking mechanisms in the K(+) channel pore as do their untethered analogs
We show here that membrane-tethered toxins facilitate the biophysical study of the roles of toxin residues in K(+) channel blockade to reveal two blocking mechanisms in the K(+) channel pore. The structure of the sea anemone type I (SAK1) toxin HmK is determined by NMR. T-HmK residues are scanned by...
| Autores principales: | , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
American Association for the Advancement of Science
2020
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7056315/ https://www.ncbi.nlm.nih.gov/pubmed/32181366 http://dx.doi.org/10.1126/sciadv.aaz3439 |