1mvi
From Proteopedia
(New page: 200px<br /><applet load="1mvi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mvi" /> '''N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTO...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1mvi.gif|left|200px]]<br /><applet load="1mvi" size=" | + | [[Image:1mvi.gif|left|200px]]<br /><applet load="1mvi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mvi" /> | caption="1mvi" /> | ||
'''N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTOXIN MVIIA, NMR, 15 STRUCTURES'''<br /> | '''N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTOXIN MVIIA, NMR, 15 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The omega-conotoxins are a set of structurally related peptides that have | + | 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== | ==About this Structure== | ||
| - | 1MVI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_magus Conus magus] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MVI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_magus Conus magus] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVI OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Conus magus]] | [[Category: Conus magus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Alewood, P | + | [[Category: Alewood, P F.]] |
| - | [[Category: Craik, D | + | [[Category: Craik, D J.]] |
| - | [[Category: Lewis, R | + | [[Category: Lewis, R J.]] |
| - | [[Category: Nielsen, K | + | [[Category: Nielsen, K J.]] |
[[Category: Thomas, L.]] | [[Category: Thomas, L.]] | ||
[[Category: NH2]] | [[Category: NH2]] | ||
| Line 22: | Line 22: | ||
[[Category: neurotoxin]] | [[Category: neurotoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:31 2008'' |
Revision as of 11:59, 21 February 2008
|
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 with as ligand. 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 Feb 21 13:59:31 2008
