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