Mapping the receptor site for charybdotoxin, a pore-blocking potassium channel inhibitor
Autor: | Roderick MacKinnon, Lise Heginbotham, Tatiana Abramson |
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Rok vydání: | 1990 |
Předmět: |
Potassium Channels
Charybdotoxin Protein Conformation Xenopus Molecular Sequence Data KcsA potassium channel Scorpion Venoms Kaliotoxin Transfection SK channel chemistry.chemical_compound Animals Amino Acid Sequence Cloning Molecular Binding Sites Scorpion toxin Inward-rectifier potassium ion channel General Neuroscience Potassium channel Electrophysiology chemistry Biochemistry Mutagenesis Site-Directed Oocytes Biophysics Ligand-gated ion channel Female |
Zdroj: | Neuron. 5:767-771 |
ISSN: | 0896-6273 |
DOI: | 10.1016/0896-6273(90)90335-d |
Popis: | 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. |
Databáze: | OpenAIRE |
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