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          Institute: MPI für medizinische Forschung     Collection: Abteilung Zellphysiologie     Display Documents

ID: 565966.0, MPI für medizinische Forschung / Abteilung Zellphysiologie
NMR structure of inactivation gates from mammalian voltage−dependent potassium channels
Translation of Title:NMR structure of inactivation gates from mammalian voltage−dependent potassium channels
Authors:Antz, Christof; Geyer, Matthias; Fakler, Bernd; Schott, Markus K.; Guy, H. Robert; Frank, Rainer; Ruppersberg, J. Peter; Kalbitzer, Hans Robert
Date of Publication (YYYY-MM-DD):1997-01-16
Title of Journal:Nature
Journal Abbrev.:Nat.
Issue / Number:6613
Start Page:272
End Page:275
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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
Last Change of the Resource (YYYY-MM-DD):--
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Abteilung Zellphysiologie
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