Journal article
Charybdotoxin block of Shaker K + channels suggests that different types of K + channels share common structural features
Neuron (Cambridge, Mass.), v 1(10), pp 997-1001
01 Dec 1988
PMID: 2483094
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Abstract
Charybdotoxin (CTX), a 37 amino acid protein isolated from the venom of L. quinquestriatus, is a high-affinity blocker of various Ca
2+-activated K
+ channels. CTX also blocks Drosophila
Shaker (
Sh) clone H4 transient K
+ currents expressed in Xenopus oocytes with similar affinity (K
d = 3.6 nM). CTX blocks both the open and the closed states of
Sh channels with no apparent change in gating behavior. In addition, the block is enhanced as the ionic strength is lowered. These properties are identical to those of CTX block of Ca
+-activated K
+ channels, and these results suggest that the external pore openings of these two functionally dissimilar K
+ channels may share common structural features.
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Details
- Title
- Charybdotoxin block of Shaker K + channels suggests that different types of K + channels share common structural features
- Creators
- Roderick MacKinnon - Brandeis UniversityPeter H. Reinhart - Brandeis UniversityMichael M. White - University of Pennsylvania
- Publication Details
- Neuron (Cambridge, Mass.), v 1(10), pp 997-1001
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Pharmacology and Physiology
- Web of Science ID
- WOS:A1988R467400010
- Scopus ID
- 2-s2.0-0024153562
- Other Identifier
- 991020837743904721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Neurosciences