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XB-ART-40488
Biochem Biophys Res Commun 2009 Oct 23;3883:490-5. doi: 10.1016/j.bbrc.2009.08.001.
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Fast inactivation in potassium channels: an interplay of cytoplasmic domains.

Sankaranarayanan K , Usman H , Mathew MK .


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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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