Crystal structure of full-length KcsA in its closed conformation

KcsA is a proton-activated, voltage-modulated K(+) channel that has served as the archetype pore domain in the Kv channel superfamily. Here, we have used synthetic antigen-binding fragments (Fabs) as crystallographic chaperones to determine the structure of full-length KcsA at 3.8 Å, as well as that...

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Bibliografische gegevens
Hoofdauteurs: Uysal, Serdar, Vásquez, Valeria, Tereshko, Valentina, Esaki, Kaori, Fellouse, Frederic A., Sidhu, Sachdev S., Koide, Shohei, Perozo, Eduardo, Kossiakoff, Anthony
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: National Academy of Sciences 2009
Onderwerpen:
Biological Sciences
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2672561/
https://ncbi.nlm.nih.gov/pubmed/19346472
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0810663106
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