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Mechanism of activation gating in the full-length KcsA K(+) channel

Using a constitutively active channel mutant, we solved the structure of full-length KcsA in the open conformation at 3.9 Å. The structure reveals that the activation gate expands about 20 Å, exerting a strain on the bulge helices in the C-terminal domain and generating side windows large enough to...

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Bibliografische gegevens
Hoofdauteurs: Uysal, Serdar, Cuello, Luis G., Cortes, D. Marien, Koide, Shohei, Kossiakoff, Anthony A., Perozo, Eduardo
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: National Academy of Sciences 2011
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC3141920/
https://ncbi.nlm.nih.gov/pubmed/21730186
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1105112108
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