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ShK Toxin,CAS#:172450-46-3,Catalog Number: K1010-V,Sequence:RSCIDTIPKSRCTAFQCKHSMKYRLSFCRKTCGTC
Various KV K+ channels. Stichodactyla Toxin blocks KV1.3, KV1.1, KV1.4, and KV1.6 at subnanomolar concentrations and KV3.2 channels at 1000-fold higher concentration than that required to inhibit KV1.3 channels.
ShK is cross-linked by three disulfide bridges: Cys3-Cys35, Cys12-Cys28, and Cys17-Cys32. The solution structure of ShK reveals two short α-helices comprising residues 14-19 and 21–24; the N-terminal eight residues adopt an extended conformation, followed by a pair of interlocking turns that resemble a 310 helix; the C-terminal Cys35 residue forms a nearly head-to-tail cyclic structure through a disulfide bond with Cys3.
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ShK Toxin,CAS#:172450-46-3,Catalog Number: K1010-V,Sequence:RSCIDTIPKSRCTAFQCKHSMKYRLSFCRKTCGTC
Various KV K+ channels. Stichodactyla Toxin blocks KV1.3, KV1.1, KV1.4, and KV1.6 at subnanomolar concentrations and KV3.2 channels at 1000-fold higher concentration than that required to inhibit KV1.3 channels.
ShK is cross-linked by three disulfide bridges: Cys3-Cys35, Cys12-Cys28, and Cys17-Cys32. The solution structure of ShK reveals two short α-helices comprising residues 14-19 and 21–24; the N-terminal eight residues adopt an extended conformation, followed by a pair of interlocking turns that resemble a 310 helix; the C-terminal Cys35 residue forms a nearly head-to-tail cyclic structure through a disulfide bond with Cys3.