Mapping the receptor site for charybdotoxin, a pore-blocking potassium channel inhibitor.
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.
Department of Cellular and Molecular Physiology, Harvard Medical School, Boston, Massachusetts 02115.
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MacKinnon
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Heginbotham
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Abramson
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D018999:Charybdotoxin; D003001:Cloning, Molecular; D004594:Electrophysiology; D005260:Female; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009865:Oocytes / Q000502:physiology; D015221:Potassium Channels / Q000737:chemistry / Q000235:genetics*; D011487:Protein Conformation; D012604:Scorpion Venoms / Q000378:metabolism* / Q000494:pharmacology; D014162:Transfection; D014981:Xenopus
D015221:Potassium Channels; D012604:Scorpion Venoms; D018999:Charybdotoxin