Structure-function relationships in potassium channels

University of Leeds (2002) J Physiol 544P, S291

Research Symposium: Structure-function relationships in potassium channels

Steve A. Goldstein and Ita O'Kelly

Departments of Pediatrics and Cellular and Molecular Physiology, Yale University, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, CT 06536, USA

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Discovered recently, K2P potassium channels (encoded by KCNK genes) are numerous, widespread and notable for their unique structure: each subunit possesses two pore-forming P domains. The channels are also remarkable in function, serving as highly regulated, potassium-selective leaks. Fundamental to the excitability of nerves and muscles, the molecular basis for leak currents had previously been a mystery. Channels in-hand, we can now consider why they remained hidden and the structural basis for their operation. Many of our most basic questions remain to be answered.




Where applicable, experiments conform with Society ethical requirements.

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