Solution structure of ω-conotoxin MVIIA using 2D NMR spectroscopy

Basus, Vladimir J. ; Nadasdi, Laszlo ; Ramachandran, J. ; Miljanich, George P. (1995) Solution structure of ω-conotoxin MVIIA using 2D NMR spectroscopy FEBS Letters, 370 (3). pp. 163-169. ISSN 0014-5793

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The solution structure of ω-conotoxin MVIIA (SNX-111), a peptide toxin from the fish hunting cone snail Conus magus and a high-affinity blocker of N-type calcium channels, was determined by 2D NMR spectroscopy. The backbones of the best 44 structures match with an average pairwise RMSD of 0.59 angstroms. The structures contain a short segment of triple-stranded β-sheet involving residues 6-8, 20-21, and 24-25. The structure of this toxin is very similar to that of ω-conotoxin GVIA with which is has only 40% sequence homology, but very similar calcium channel binding affinity and selectivity.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Neurotoxin; Calcium Channel Blocker; NMR Structure; Complete Relaxation Matrix; Conus magus
ID Code:40737
Deposited On:25 May 2011 05:29
Last Modified:25 May 2011 05:29

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