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
Full text not available from this repository.
Official URL: http://linkinghub.elsevier.com/retrieve/pii/001457...
Related URL: http://dx.doi.org/10.1016/0014-5793(95)00819-U
Abstract
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 |
Repository Staff Only: item control page
