Solution structure of omega-conotoxin MVIIC, a high affinity ligand of P-type calcium channels, using 1H NMR spectroscopy and complete relaxation matrix analysis.

Abstract

We have determined the solution structure of the omega-conotoxin MVIIC from Conus magus by 1H NMR. This conopeptide preferentially blocks P and Q type Ca2+ currents by binding with high affinity to voltage-sensitive Ca2+ channels in neurons. This 26 residue peptide with three disulfide bonds was chemically synthesized and refolded for NMR structural studies… (More)

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Cite this paper

@article{FarrJones1995SolutionSO, title={Solution structure of omega-conotoxin MVIIC, a high affinity ligand of P-type calcium channels, using 1H NMR spectroscopy and complete relaxation matrix analysis.}, author={Shauna Farr-Jones and George P. Miljanich and L{\'a}szl{\'o} N{\'a}dasdi and Janani Ramachandran and Vladimir J. Basus}, journal={Journal of molecular biology}, year={1995}, volume={248 1}, pages={106-24} }