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Article

Interaction of Ca2(+)-activated K+ channels with refolded charybdotoxins mutated at a central interaction residue.

Neuropharmacology - 1 Jan 1996

Naini A A, Shimony E, Kozlowski E, Shaikh T, Dang W, Miller C

Abstract excerpt

Charybdotoxin is a small peptide blocker of K+ channels, rigidly held in 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 epsilon-amino group into the...

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Identifiers

PMID: 8938722
DOI: 10.1016/0028-3908(96)00112-8

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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