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• W1992534248 abstract "Charybdotoxin is a small peptide blocker of K+ channels, rigidly held in an active conformation by three disulfide bonds. The toxin blocks K+ channels by binding to a receptor site located at the external “vestibule”, and thus physically occluding the outer opening of the K+ conduction pore. In the blocked complex, K27, a residue on the toxin's molecular surface, projects its ϵ-amino group into the K+-selective pore. The results here show that CTX, produced by heterologous expression in E. coli, may be manipulated to place unnatural positively charged residues at position 27. The toxin folds faithfully to its native conformation when the crucial lysine at position 27 is replaced by a cysteine residue, a maneuver that allows specific chemical modification of this side-chain. Replacements of K27 by side-chains slightly shorter or slightly longer than lysine yield active toxins. The toxin variant with ornithine at this position interacts much less strongly with K+ ions in the pore of slowpoke-type Ca2+-activated K+ channels than does wild-type toxin. This result argues that the ϵ-amino group of K27 in bound toxin lies only a fewångstroms away from a K+ ion occupying the blocked pore. The peptide folds with high efficiency to form the correct disulfides even in the presence of strong denaturants. Copyright © 1996 Published by Elsevier Science Ltd" @default.
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• W1992534248 date "1996-01-01" @default.
• W1992534248 modified "2023-10-17" @default.
• W1992534248 title "Interaction of Ca 2+ -activated K + Channels with Refolded Charybdotoxins Mutated at a Central Interaction Residue" @default.
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• W1992534248 doi "https://doi.org/10.1016/0028-3908(96)00112-8" @default.
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