1MVI
N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTOXIN MVIIA, NMR, 15 STRUCTURES
Summary for 1MVI
| Entry DOI | 10.2210/pdb1mvi/pdb |
| Descriptor | MVIIA (1 entity in total) |
| Functional Keywords | conus magus peptide specific to n-type voltage sensitive calcium channel, neurotoxin |
| Biological source | Conus magus (magus cone) |
| Cellular location | Secreted : P05484 |
| Total number of polymer chains | 1 |
| Total formula weight | 2650.22 |
| Authors | Nielsen, K.J.,Thomas, L.,Lewis, R.J.,Alewood, P.F.,Craik, D.J. (deposition date: 1996-08-02, release date: 1997-08-12, Last modification date: 2024-11-20) |
| Primary citation | Nielsen, K.J.,Thomas, L.,Lewis, R.J.,Alewood, P.F.,Craik, D.J. A consensus structure for omega-conotoxins with different selectivities for voltage-sensitive calcium channel subtypes: comparison of MVIIA, SVIB and SNX-202. J.Mol.Biol., 263:297-310, 1996 Cited by PubMed Abstract: The omega-conotoxins are a set of structurally related peptides that have a wide range of specificities for different subtypes of the voltage-sensitive calcium channel (VSCC). To understand their VSCC subtype differentiation we studied the structure of two naturally occurring omega-conotoxins, MVIIA (specific to N-type) and SVIB (specific to P/Q-type) and a synthetic hybrid, SNX-202, which has altered specificities to both VSCC subtypes. The secondary structures of the three peptides are almost identical, consisting of a triple-stranded beta-sheet and several turns. A comparison of NMR data emphasizes the structural similarities between the peptides and highlights some minor structural differences. In the three-dimensional structures of SVIB and MVIIA these are manifested as orientational differences between two key loops. The structural rigidity of MVIIA was also examined. H alpha shifts are similar in a range of solvents, indicating that there are no solvent-induced changes in structure. The omega-conotoxins form a consensus structure despite differences in sequence and VSCC subtype specificity. This indicates that the omega-conotoxin macrosites for the N/P/Q-subfamily of VSCCs are related, with specificity for receptor targets being conferred by the positions of functional side-chains on the surface of the peptides. PubMed: 8913308DOI: 10.1006/jmbi.1996.0576 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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