1mvj
From Proteopedia
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|PDB= 1mvj |SIZE=350|CAPTION= <scene name='initialview01'>1mvj</scene> | |PDB= 1mvj |SIZE=350|CAPTION= <scene name='initialview01'>1mvj</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvj OCA], [http://www.ebi.ac.uk/pdbsum/1mvj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mvj RCSB]</span> | ||
}} | }} | ||
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[[Category: Nielsen, K J.]] | [[Category: Nielsen, K J.]] | ||
[[Category: Thomas, L.]] | [[Category: Thomas, L.]] | ||
| - | [[Category: NH2]] | ||
[[Category: conus striatus peptide specific to p/q-type voltage sensitive calcium channel]] | [[Category: conus striatus peptide specific to p/q-type voltage sensitive calcium channel]] | ||
[[Category: neurotoxin]] | [[Category: neurotoxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:21:41 2008'' |
Revision as of 19:21, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTOXIN MVIIA NMR, 15 STRUCTURES
Overview
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.
About this Structure
1MVJ is a Single protein structure of sequence from Conus striatus. Full crystallographic information is available from OCA.
Reference
A consensus structure for omega-conotoxins with different selectivities for voltage-sensitive calcium channel subtypes: comparison of MVIIA, SVIB and SNX-202., Nielsen KJ, Thomas L, Lewis RJ, Alewood PF, Craik DJ, J Mol Biol. 1996 Oct 25;263(2):297-310. PMID:8913308
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