Solution structure of α-conotoxin SI

Andrew J. Benie, David Whitford, Balazs Hargittai, George Barany, Robert W. Janes

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


The nuclear magnetic resonance solution structure of α-conotoxin SI has been determined at pH 4.2. The 36 lowest energy structures show that α-conotoxin SI exists in a single major solution conformation and is stabilized by six hydrogen bonds. Comparisons are made between the SI solution structure and the solution and crystal structures of α-conotoxin GI. Surprisingly, a high degree of similarity between the backbone conformations of the GI crystal and the SI solution structures is seen in the region of lowest sequence homology, namely residues Gly-8 to Ser-12. This similarity is more surprising when considering that in SI a proline replaces the Arg-9 found in GI. The correspondence in conformation in this region provides the definitive evidence that it is the loss of the arginine basic charge at residue 9 which determines the differences in toxicity between GI and SI, rather than any changes in conformation induced by the cyclic proline residue. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)287-295
Number of pages9
JournalFEBS Letters
Issue number3
StatePublished - Jul 7 2000


  • Circular dichroism
  • Conotoxin
  • Disulfide linked peptide
  • Nicotinic acetylcholine receptor
  • Nuclear magnetic resonance
  • Three-dimensional structure

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