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Solution structure and function of the "tandem inactivation domain" of the neuronal A-type potassium channel Kv1.4

Wissmann, Ralph and Bildl, Wolfgang and Oliver, Dominik and Beyermann, Michael and Kalbitzer, Hans Robert and Bentrop, Detlef and Fakler, Bernd (2003) Solution structure and function of the "tandem inactivation domain" of the neuronal A-type potassium channel Kv1.4. The Journal of biological chemistry 278 (18), pp. 16142-16150.

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Abstract

Cumulative inactivation of voltage-gated (Kv) K(+) channels shapes the presynaptic action potential and determines timing and strength of synaptic transmission. Kv1.4 channels exhibit rapid "ball-and-chain"-type inactivation gating. Different from all other Kvalpha subunits, Kv1.4 harbors two inactivation domains at its N terminus. Here we report the solution structure and function of this ...

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Item Type:Article
Date:2003
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
12590144PubMed ID
10.1074/jbc.M210191200DOI
Classification:
NotationType
Amino Acid SequenceMESH
AnimalsMESH
CHO CellsMESH
CricetinaeMESH
Kv1.4 Potassium ChannelMESH
Molecular Sequence DataMESH
Neuronal PlasticityMESH
Neurons/metabolismMESH
Nuclear Magnetic Resonance, BiomolecularMESH
Potassium Channels/physiologyMESH
Potassium Channels, Voltage-GatedMESH
Protein Structure, SecondaryMESH
SolutionsMESH
Structure-Activity RelationshipMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Yes
Owner: Gertraud Kellers
Deposited On:15 Sep 2010 09:19
Last Modified:15 Sep 2010 09:19
Item ID:16589
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