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Summary

Description A protein NMR structure of the four-disulfide-bridge scorpion toxin maurotoxin, 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. The maurotoxin disulfide bridge connectivity is uncommon among 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 1TXM using PyMol
Author Opabinia regalis
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8 March 2007

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current04:14, 9 March 2007Thumbnail for version as of 04:14, 9 March 2007666 × 810 (318 KB)Opabinia regalis{{Information |Description=A protein NMR structure of the four-disulfide-bridge scorpion toxin maurotoxin, which inhibits potassium ion channels. The protein backbone is shown in red, the alpha carbons of the eight cysteine residues are shown in green, an

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