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...

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Detalles Bibliográficos
Autores principales: Zhao, Ruiming, Dai, Hui, Mendelman, Netanel, Chill, Jordan H., Goldstein, Steve A. N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2020
Materias:
Research Articles
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

Internet

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

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