1mvi
From Proteopedia
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| - | [[Image:1mvi.gif|left|200px]] | + | [[Image:1mvi.gif|left|200px]] |
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| - | '''N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTOXIN MVIIA, NMR, 15 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1mvi |SIZE=350|CAPTION= <scene name='initialview01'>1mvi</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTOXIN MVIIA, NMR, 15 STRUCTURES''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MVI is a [ | + | 1MVI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Conus_magus Conus magus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVI OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8913308 8913308] |
[[Category: Conus magus]] | [[Category: Conus magus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: neurotoxin]] | [[Category: neurotoxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:48:40 2008'' |
Revision as of 10:48, 20 March 2008
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| 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
1MVI is a Single protein structure of sequence from Conus magus. 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
Page seeded by OCA on Thu Mar 20 12:48:40 2008
