Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K+ channel
نویسندگان
چکیده
منابع مشابه
Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K+ channel
Pore-blocking toxins inhibit voltage-dependent K(+) channels (Kv channels) by plugging the ion-conduction pathway. We have solved the crystal structure of paddle chimera, a Kv channel in complex with charybdotoxin (CTX), a pore-blocking toxin. The toxin binds to the extracellular pore entryway without producing discernable alteration of the selectivity filter structure and is oriented to projec...
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in membrane voltage, this kind of ion channel undergoes a conformational change that opens the ion conduction pathway. The Shaker K ϩ channel from Drosophila mela-shaking phenotype of flies in which the channel gene is mutated. It is interesting that two of the early described shaking phenotypes of Drosophila, the hyperkinetic mutants , result from mutations in a K ϩ channel  subunit Summary g...
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Voltage-dependent gating in K(+) channels results from the mechanical coupling of voltage sensor movements to pore opening. We used single and double mutations in the pore of the Shaker K(+) channel to analyze a late concerted pore opening transition and interpreted the results in the context of known K(+) channel structures. Gating sensitive mutations are located at mechanistically informative...
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Voltage-activated K+ channels are integral membrane proteins that open or close a K(+)-selective pore in response to changes in transmembrane voltage. Although the S4 region of these channels has been implicated as the voltage sensor, little is known about how opening and closing of the pore is accomplished. We explored the gating process by introducing cysteines at various positions thought to...
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X-ray crystallography has made considerable recent progress in providing static structures of ion channels. Here we describe a complementary method-systematic fluorescence scanning-that reveals the structural dynamics of a channel. Local protein motion was measured from changes in the fluorescent intensity of a fluorophore attached at one of 37 positions in the pore domain and in the S4 voltage...
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ژورنال
عنوان ژورنال: eLife
سال: 2013
ISSN: 2050-084X
DOI: 10.7554/elife.00594