Solution structure determination by two-dimensional 1H NMR of omega-conotoxin MVIID, a calcium channel blocker peptide

Biochem Biophys Res Commun. 1999 Jan 8;254(1):32-5. doi: 10.1006/bbrc.1998.9878.


The three-dimensional structure of omega-conotoxin MVIID has been determined in aqueous solution by two-dimensional 1H NMR techniques. A total of 267 relevant upper-bound distance restraints were used to obtain a family of convergent structures using molecular dynamics methods. A standard simulated annealing protocol using the XPLOR program included in ARIA provided a total of 18 final structures. The averaged RMSD between these structures and the mean atomic coordinates was 0.8 +/- 0.3 A for the backbone atoms. The highest mobility was observed in the segments between residues 10 to 13, comprising Tyr 13, one of the residues shown to be important for binding of omega-conotoxin GVIA and MVIIA to N-type calcium channels. The three-dimensional structure is stabilised by the three disulfide bonds and includes a short antiparallel beta-strand between residues 5-8, 23-25 and 19-21. The folding for this non-N-type calcium channel blocker is similar to that previously calculated for omega-conotoxins GVIA, MVIIA and MVIIC. This suggests the disulfide bond pattern fixes the structure. The reported three-dimensional information can be used to advantage in order to highlight the structural parameters involved in discrimination among calcium channel subtypes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium Channel Blockers / chemistry*
  • Conotoxins*
  • Magnetic Resonance Spectroscopy
  • Mollusk Venoms
  • Peptides / chemistry*
  • Protein Conformation*


  • Calcium Channel Blockers
  • Conotoxins
  • Mollusk Venoms
  • Peptides
  • omega-conotoxin MVIID