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Summary

Description A protein NMR structure of the four-disulfide-bridge scorpion toxin HsTx1, which inhibits potassium ion channels. The protein backbone is shown in red, the alpha carbons of the eight cysteine residues are shown in green, and the disulfide bridges themselves are shown in yellow. This disulfide bridge connectivity is characteristic of many scorpion toxins. Multiple structures are shown to reflect the natural fluctuations in native-state protein structure in solution.
Date
Source Self-created from PDB ID 1QUZ using PyMol
Author Opabinia regalis
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8 March 2007

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current04:11, 9 March 2007Thumbnail for version as of 04:11, 9 March 2007666 × 810 (408 KB)Opabinia regalis{{Information |Description=A protein NMR structure of the four-disulfide-bridge scorpion toxin HsTx1, which inhibits potassium ion channels. The protein backbone is shown in red, the alpha carbons of the eight cysteine residues are shown in green, and the

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