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

Antz, C. and Geyer, M. and Fakler, B. and Schott, M. K. and Guy, H. R. and Franke, R. and Ruppersberg, J. P. and Kalbitzer, Hans Robert (1997) NMR structure of inactivation gates from mammalian voltage-dependent potassium channels. Nature 385 (6613), pp. 272-275.

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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 ...

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Item Type:Article
Date:1997
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
9000078PubMed ID
10.1038/385272a0DOI
Classification:
NotationType
Amino Acid SequenceMESH
AnimalsMESH
ElectrochemistryMESH
Ion Channel GatingMESH
Magnetic Resonance SpectroscopyMESH
MammalsMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Peptide Fragments/chemistryMESH
Potassium Channels/chemistryMESH
Protein ConformationMESH
Structure-Activity RelationshipMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:13 Sep 2010 08:15
Last Modified:13 Sep 2010 08:15
Item ID:16551
Owner Only: item control page
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