A point mutation in a Shaker K+ channel changes its charybdotoxin binding site from low to high affinity
- 1 April 1992
- journal article
- research article
- Published by Elsevier in Biophysical Journal
- Vol. 62 (1) , 5-7
- https://doi.org/10.1016/s0006-3495(92)81760-5
Abstract
No abstract availableKeywords
This publication has 8 references indexed in Scilit:
- Design, synthesis, and functional expression of a gene for charybdotoxin, a peptide blocker of K+ channels.Proceedings of the National Academy of Sciences, 1991
- Three‐dimensional structure of natural charybdotoxin in aqueous solution by 1H‐NMR Charybdotoxin possesses a structural motif found in other scorpion toxinsEuropean Journal of Biochemistry, 1991
- Mapping the receptor site for charybdotoxin, a pore-blocking potassium channel inhibitorNeuron, 1990
- Mutations Affecting Tea Blockade and Ion Permeation in Voltage-activated K + ChannelsScience, 1990
- Competition for block of a Ca2+-activated K+ channel by charybdotoxin and tetraethylammoniumNeuron, 1988
- Mechanism of charybdotoxin block of the high-conductance, Ca2+-activated K+ channel.The Journal of general physiology, 1988
- Sequence of a Probable Potassium Channel Component Encoded at Shaker Locus of DrosophilaScience, 1987
- Rapid and efficient site-specific mutagenesis without phenotypic selection.Proceedings of the National Academy of Sciences, 1985