Schott, M. K. and Antz, C. and Frank, R. and Ruppersberg, J. P. and Kalbitzer, Hans R. (1998) Structure of the inactivating gate from the Shaker voltage gated K+ channel analyzed by NMR spectroscopy. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 27 (2). pp. 99-104. ISSN 0175-7571, 1432-1017
Full text not available from this repository.Abstract
Rapid inactivation of voltage-gated K+ (K-v) 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 K-v channels are also biologically active when synthesized separately and added as a peptide to the solution. Synthetic inactivating ball domains from different K-v channels with hardly any sequence homology mediate quite similar effects even on unrelated K-v channel subtypes whose inactivation domain has been deleted. The solution structure of the inactivating ball peptide from Shaker (Sh-P22) was analyzed with NMR spectroscopy. The NMR data indicate a non-random structure in an aqueous environment. However, while other inactivating ball peptides showed well-defined three-dimensional structures under these conditions, Sh-P22 does not have a unique, compactly folded structure in solution.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | POTASSIUM CHANNEL; COUPLING-CONSTANTS; MAMMALIAN BRAIN; IK(A) CHANNELS; RAT-BRAIN; PROTEINS; SPECTRA; DROSOPHILA; PEPTIDES; DOMAINS; Shaker; potassium-channel; NMR; structure |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 01 Mar 2023 07:48 |
| Last Modified: | 01 Mar 2023 07:48 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50191 |
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