NMR structure of inactivation gates from mammalian voltage-dependent potassium channels

Christof Antz, Matthias Geyer, Bernd Fakler, Markus K. Schott, H. Robert Guy, Rainer Frank, Johann Peter Ruppersberg and Hans Robert Kalbitzer
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Christof Antz: University of Tübingen
Matthias Geyer: Max-Planck-Institute for Medical Research
Bernd Fakler: University of Tübingen
Markus K. Schott: University of Tübingen
H. Robert Guy: National Institute of Health
Rainer Frank: Im Neuenheimer Feld
Johann Peter Ruppersberg: University of Tübingen
Hans Robert Kalbitzer: Max-Planck-Institute for Medical Research

Nature, 1997, vol. 385, issue 6613, 272-275

Abstract: Abstract The electrical signalling properties of neurons originate largely from the gating properties of their ion channels. N-type inactivation of voltage-gated potassium (Kv) channels is the best-understood gating transition in ion channels, and occurs by a 'ball-and-chain' type mechanism. In this mechanism an N-terminal domain (inactivation gate), which is tethered to the cytoplasmic side of the channel protein by a protease-cleavable chain, binds to its receptor at the inner vestibule of the channel, thereby physically blocking the pore1,2. Even when synthesized as a peptide, ball domains restore inactivation in Kv channels whose inactivation domains have been deleted2,3. Using high-resolution nuclear magnetic resonance (NMR) spectroscopy, we analysed the three-dimensional structure of the ball peptides from two rapidly inactivating mammalian Kv channels (Raw3 (Kv3.4) and RCK4 (Kvl.4)). The inactivation peptide of Raw3 (Raw3-IP) has a compact structure that exposes two phosphorylation sites and allows the formation of an intramolecular disulphide bridge between two spatially close cysteine residues. Raw3-IP exhibits a characteristic surface charge pattern with a positively charged, a hydrophobic, and a negatively charged region. The RCK4 inactivation peptide (RCK4-IP) shows a similar spatial distribution of charged and uncharged regions, but is more flexible and less ordered in its amino-terminal part.

Date: 1997
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DOI: 10.1038/385272a0

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