Abstract
The Shaker K+ channel belongs to a family of structurally related voltage-activated cation channels that play a central role in cellular electrical signaling. By studying multiple site-directed mutants of the Shaker K+ channel, a region that forms the binding site for a pore-blocking scorpion toxin has been identified. The region contains a sequence that is highly conserved among cloned K+ channels and may contribute to the formation of the ion conduction pore.
Publication types
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Binding Sites
-
Charybdotoxin
-
Cloning, Molecular
-
Electrophysiology
-
Female
-
Molecular Sequence Data
-
Mutagenesis, Site-Directed
-
Oocytes / physiology
-
Potassium Channels / chemistry
-
Potassium Channels / genetics*
-
Protein Conformation
-
Scorpion Venoms / metabolism*
-
Scorpion Venoms / pharmacology
-
Transfection
-
Xenopus
Substances
-
Potassium Channels
-
Scorpion Venoms
-
Charybdotoxin