Article
Crystal structure of full-length KcsA in its closed conformation.
Proceedings of the National Academy of Sciences of the United States of America - 21 Apr 2009
Uysal Serdar, Vásquez Valeria, Tereshko Valentina, Esaki Kaori, Fellouse Frederic A, Sidhu Sachdev S, Koide Shohei, Perozo Eduardo, Kossiakoff Anthony
Abstract excerpt
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 A, as well as that of its isolated C-terminal domain at 2.6 A. The structure of the full-length KcsA-Fab complex reveals a...
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