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• W2046281646 endingPage "442" @default.
• W2046281646 startingPage "431" @default.
• W2046281646 abstract "Kv4 voltage-gated K(+) channels are responsible for transient K(+) currents in the central nervous system and in the heart. HpTx2 is a peptide toxin that selectively inhibits these currents; making it a useful probe for understanding Kv4 channel structure and drug binding. Therefore, we developed a method to produce large amounts of recombinant HpTx2. Recombinant toxin inhibits all three Kv4 isoforms to the same degree; however, the voltage-dependence of inhibition is less apparent for Kv4.1 than for Kv4.3. Similarly, recombinant HpTx2(GS) effects gating characteristics of both channels, but Kv4.1 to a much lesser degree. The toxin lacks affinity for Kv1.4, Kv2.1, and Kv3.4. To locate the binding site, the amino acids linking the third and forth membrane spanning segments of Kv4.3 were replaced with analogous amino acids of Kv1.4. The chimeric K(+) channel was completely insensitive to block by rHpTx2, suggesting that its binding site is near the channel's voltage sensor. These data show that rHpTx2(GS) is a gating modifier toxin that binds to a site remote from the pore." @default.
• W2046281646 created "2016-06-24" @default.
• W2046281646 creator A5005670100 @default.
• W2046281646 creator A5058017240 @default.
• W2046281646 creator A5072134023 @default.
• W2046281646 creator A5073341372 @default.
• W2046281646 date "2005-03-01" @default.
• W2046281646 modified "2023-09-23" @default.
• W2046281646 title "Heteropoda toxin 2 is a gating modifier toxin specific for voltage-gated K+ channels of the Kv4 family" @default.
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• W2046281646 doi "https://doi.org/10.1016/j.toxicon.2004.11.015" @default.
• W2046281646 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15733564" @default.
• W2046281646 hasPublicationYear "2005" @default.
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