Science. 1990 Oct 26;250(4980):568-71.

Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB.

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Department of Molecular and Cellular Physiology, Stanford University School of Medicine, CA 94305.

Abstract

Site-directed mutagenesis experiments have suggested a model for the inactivation mechanism of Shaker potassium channels from Drosophila melanogaster. In this model, the first 20 amino acids form a cytoplasmic domain that interacts with the open channel to cause inactivation. The model was tested by the internal application of a synthetic peptide, with the sequence of the first 20 residues of the ShB alternatively spliced variant, to noninactivating mutant channels expressed in Xenopus oocytes. The peptide restored inactivation in a concentration-dependent manner. Like normal inactivation, peptide-induced inactivation was not noticeably voltage-dependent. Trypsin-treated peptide and peptides with sequences derived from the first 20 residues of noninactivating mutants did not restore inactivation. These results support the proposal that inactivation occurs by a cytoplasmic domain that occludes the ion-conducting pore of the channel.

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Science. 1990 Oct 26;250(4980):506-7.

PMID:: 2122520; [PubMed - indexed for MEDLINE]

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Biophysical and molecular mechanisms of Shaker potassium channel inactivation. [Science. 1990]
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