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...
Topics
- Amino Acid Sequence
- Conotoxins
- Inhibitory Concentration 50
- Leucine
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Peptide Fragments
- Potassium Channel Blockers
- Potassium Channels
- Protein Structure, Tertiary
- Sequence Alignment