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| ID:
565674.0,
MPI für medizinische Forschung / Abteilung Biophysik |
| 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 | | Language: | English | | Date of Publication (YYYY-MM-DD): | 1997-01-16 | | Title of Journal: | Nature | | Journal Abbrev.: | Nat. | | Volume: | 385 | | 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
| | Identifiers: | LOCALID:5429
URI:http%3A%2F%2Fwww.nature.com%2Fcgi-taf%2FDynaPage.t...
URI:http%3A%2F%2Fwww.nature.com%2Fcgi-taf%2FDynaPage.t...
DOI:10.1038%2F385272a0 |
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