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NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1

Wissmann, R. ; Baukrowitz, T. ; Kalbacher, H. ; Kalbitzer, Hans Robert ; Ruppersberg, J. P. ; Pongs, O. ; Antz, C. ; Fakler, B.



Abstract

Rapid N-type inactivation of voltage-dependent potassium (Kv) channels controls membrane excitability and signal propagation in central neurons and is mediated by protein domains (inactivation gates) occluding the open channel pore from the cytoplasmic side. Inactivation domains (ID) are donated either by the pore-forming alpha-subunit or certain auxiliary beta-subunits. Upon coexpression, ...

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