Neuron
ArticleInternal blockade of a Ca2+-activated K+ channel by shaker B inactivating “ball” peptide
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Cited by (49)
N-type inactivation of the potassium channel KcsA by the Shaker B "ball" Peptide: Mapping the inactivating peptide-binding epitope
2008, Journal of Biological ChemistryCitation Excerpt :The Inactivating ShB Peptide Uncouples and Inactivates KcsA—The prokaryotic potassium channel KcsA behaves in many respects similarly to its structurally more complex eukaryotic counterparts (46), including the occurrence of slow, C-type inactivation (47). Perhaps for these reasons and also because of the promiscuity of the ShB ball peptide in inducing N-type, rapid inactivation in many different potassium channels (4–10), it has been assumed that the ShB peptide should also induce N-type inactivation in KcsA (13). Nonetheless, no experimental evidence on this matter has been reported to date.
N-type Inactivation Features of Kv4.2 Channel Gating
2004, Biophysical JournalCitation Excerpt :The hydrophobicity of this initial part of the N-terminus seems to be essential for binding within the channel, with no absolute requirement for sequence similarities (Murrell-Lagnado and Aldrich, 1993a). In accordance with previous results obtained with ShB peptide applied to Kv2.1 (Isacoff et al., 1991) and large conductance Ca2+-activated K+ channels (Foster et al., 1992; Toro et al., 1992), our peptide application experiments showed that this reaction is not subfamily-specific. Positively charged residues in a region next to the proximal hydrophobic inactivation domain may influence the blocking reaction by long-range electrostatic interactions in Shaker channels (Murrell-Lagnado and Aldrich, 1993a,b) or may directly interact with parts of the channel protein outside the pore (Gulbis et al., 2000).
Potassium ion channel inactivation peptides
1999, Methods in EnzymologyA mammalian transient type K<sup>+</sup> channel, Rat Kv1.4, Has two potential domains that could produce rapid inactivation
1997, Journal of Biological ChemistryBall-and-Chain Inactivation in Potassium Channels
2023, Annual Review of Biophysics