| Fast inactivation in potassium channels: an interplay of cytoplasmic domains. | |
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MedLine Citation:
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PMID: 19665007 Owner: NLM Status: In-Process |
Abstract/OtherAbstract:
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Fast inactivation in voltage-gated potassium channels has traditionally been associated exclusively with the N-terminus. Here, we explore the role of the T1 domain using a series of chimeric channels. A chimeric channel, 4N/2, (N-terminus from the rapidly inactivating hKv1.4, and the channel body from the non-inactivating hKv1.2), exhibited slower and incomplete inactivation as compared to the wild-type hKv1.4. Replacing the T1 domain of 4N2 with that from hKv1.2 (4N/2T1/2), restored inactivation, while that from hKv1.1 (4N/1T1/2) completely abolished inactivation. Based on these observations, we hypothesize a correlation between the tetramerization domain and the putative inactivation domain receptor in the process of rapid inactivation of hKv1 channels. |
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Authors:
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Kavitha Sankaranarayanan; Hyder Usman; M K Mathew |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2009-08-05 |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: 388 ISSN: 1090-2104 ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 2009 Oct |
Date Detail:
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Created Date: 2009-09-08 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: United States |
Other Details:
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Languages: eng Pagination: 490-5 Citation Subset: IM |
Affiliation:
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National Centre for Biological Sciences, Tata Institute of Fundamental Research, UAS-GKVK Campus, GKVK P.O., Bangalore 560065, India. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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