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Article

KappaM-conotoxin RIIIK, structural and functional novelty in a K+ channel antagonist.

Biochemistry - 13 Jul 2004

Al-Sabi Ahmed, Lennartz Dirk, Ferber Michael, Gulyas Jozsef, Rivier Jean E F, Olivera Baldomero M, Carlomagno Teresa, Terlau Heinrich

Abstract excerpt

Venomous organisms have evolved a variety of structurally diverse peptide neurotoxins that target ion channels. Despite the lack of any obvious structural homology, unrelated toxins that interact with voltage-activated K(+) channels share a dyad motif composed of a lysine and a hydrophobic amino acid residue, usually a phenylalanine or a tyrosine. kappaM-Conotoxin RIIIK (kappaM-RIIIK), recently characterized from...

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PMID: 15236570
DOI: 10.1021/bi0495681

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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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