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J. Biol. Chem., Vol. 278, Issue 18, 16142-16150, May 2, 2003

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 278/18/16142    most recent M210191200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Wissmann, R. Articles by Fakler, B. Search for Related Content PubMed PubMed Citation Articles by Wissmann, R. Articles by Fakler, B. Social Bookmarking                      What's this?

Solution Structure and Function of the "Tandem Inactivation Domain" of the Neuronal A-type Potassium Channel Kv1.4^*,

Ralph Wissmann, Wolfgang Bildl, Dominik Oliver, Michael Beyermann^§, Hans-Robert Kalbitzer^¶, Detlef Bentrop, and Bernd Fakler

From the  Department of Physiology II, University of Freiburg, Hermann-Herder-Strasse 7, 79104 Freiburg, Germany, ^§ Forschungsinstitut für Molekulare Pharmakologie, Campus Berlin-Buch, Robert-Rössle-Strasse 10, 13125 Berlin, Germany, and ^¶ Department of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany

Cumulative inactivation of voltage-gated (Kv) K⁺ channels shapes the presynaptic action potential and determines timing and strength of synaptic transmission. Kv1.4 channels exhibit rapid "ball-and-chain"-type inactivation gating. Different from all other Kv subunits, Kv1.4 harbors two inactivation domains at its N terminus. Here we report the solution structure and function of this "tandem inactivation domain" using NMR spectroscopy and patch clamp recordings. Inactivation domain 1 (ID1, residues 1-38) consists of a flexible N terminus anchored at a 5-turn helix, whereas ID2 (residues 40-50) is a 2.5-turn helix made up of small hydrophobic amino acids. Functional analysis suggests that only ID1 may work as a pore-occluding ball domain, whereas ID2 most likely acts as a "docking domain" that attaches ID1 to the cytoplasmic face of the channel. Deletion of ID2 slows inactivation considerably and largely impairs cumulative inactivation. Together, the concerted action of ID1 and ID2 may promote rapid inactivation of Kv1.4 that is crucial for the channel function in short term plasticity.

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