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

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Antz,  Christof
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Geyer,  Matthias
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Schott,  Markus K.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Ruppersberg,  J. Peter
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Kalbitzer,  Hans Robert
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Antz, C., Geyer, M., Fakler, B., Schott, M. K., Guy, H. R., Frank, R., et al. (1997). NMR structure of inactivation gates from mammalian voltage-dependent potassium channels. Nature, 385(6613), 272-275. doi:10.1038/385272a0.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-AF70-A
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 pore. Even when synthesized as a peptide, ball domains restore inactivation in Kv channels whose inactivation domains have been deleted. Using high-resolution nuclear magnetic resonance (NMR) spectroscopy, we analysed the three-dimensional structure of the ball peptides from two rapidly inactivating mammalian K. channels (Raw3 (Kv3.4) and RCK4 (Kv1.4)). 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.