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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-AF70-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-77DE-C
Genre: Journal Article
Alternative Title : NMR structure of inactivation gates from mammalian voltage-dependent potassium channels

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Antz, Christof1, Author              
Geyer, Matthias1, Author              
Fakler, Bernd, Author
Schott, Markus K.1, Author              
Guy, H. Robert, Author
Frank, Rainer, Author
Ruppersberg, J. Peter2, Author              
Kalbitzer, Hans Robert1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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 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.

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Language(s): eng - English
 Dates: 1996-09-111996-11-201997-01-16
 Publication Status: Published in print
 Pages: 4
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 Rev. Type: Peer
 Identifiers: eDoc: 666087
DOI: 10.1038/385272a0
URI: http://www.ncbi.nlm.nih.gov/pubmed/9000078
Other: 5429
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Title: Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 385 (6613) Sequence Number: - Start / End Page: 272 - 275 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238