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Structure of the inactivating gate from the Shaker voltage gated K⁺ channel analyzed by NMR spectroscopy

Schott, M. K. and Antz, C. and Frank, R. and Ruppersberg, J. P. and Kalbitzer, Hans Robert (1998) Structure of the inactivating gate from the Shaker voltage gated K⁺ channel analyzed by NMR spectroscopy. European biophysics journal : EBJ 27 (2), pp. 99-104.

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Abstract

Rapid inactivation of voltage-gated K+ (Kv) channels is mediated by an N-terminal domain (inactivating ball domain) which blocks the open channel from the cytoplasmic side. Inactivating ball domains of various Kv channels are also biologically active when synthesized separately and added as a peptide to the solution. Synthetic inactivating ball domains from different Kv channels with hardly any ...

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Item Type:Article
Date:1998
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
9530825PubMed ID
Classification:
NotationType
Amino Acid SequenceMESH
ElectrophysiologyMESH
Ion Channel Gating/physiologyMESH
Molecular Sequence DataMESH
Nuclear Magnetic Resonance, BiomolecularMESH
Peptides/physiologyMESH
Potassium Channels/physiologyMESH
Shaker Superfamily of Potassium ChannelsMESH
ThermodynamicsMESH
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 08:09
Last Modified:13 Sep 2010 08:09
Item ID:16555
Owner Only: item control page
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