1b45
From Proteopedia
(New page: 200px<br /><applet load="1b45" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b45" /> '''ALPHA-CNIA CONOTOXIN FROM CONUS CONSORS, NMR...) |
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| - | [[Image:1b45.gif|left|200px]]<br /><applet load="1b45" size=" | + | [[Image:1b45.gif|left|200px]]<br /><applet load="1b45" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1b45" /> | caption="1b45" /> | ||
'''ALPHA-CNIA CONOTOXIN FROM CONUS CONSORS, NMR, 43 STRUCTURES'''<br /> | '''ALPHA-CNIA CONOTOXIN FROM CONUS CONSORS, NMR, 43 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Two novel alpha-conotoxins were purified and characterized from the venom | + | Two novel alpha-conotoxins were purified and characterized from the venom of the fish-hunting cone snail Conus consors. These peptides were identified by screening HPLC fractions of the crude venom and by binding experiments with Torpedo nicotinic acetylcholine receptor. The toxins named alpha-CnIA and alpha-CnIB exhibited sequences of 14 and 12 amino acids, respectively. The alpha-CnIA represents the main alpha-conotoxin contained in the venom, whereas alpha-CnIB is present in a relatively small amount. Chemical synthesis of alpha-CnIA was carried out using the Fmoc methodology by selective disulfide bond formation. The biological activity of the toxin was assessed in fish and mice. The alpha-CnIA inhibited the fixation of iodinated alpha-bungarotoxin to Torpedo nicotinic acetylcholine receptors with an IC50 of 0.19 microM which can be compared to the IC50 of 0.31 microM found for the previously characterized alpha-MI isolated from the piscivorous Conus magus. The synthetic alpha-CnIA blocked spontaneous and evoked synaptic potentials in frog and mouse isolated neuromuscular preparations at sub-micromolar concentrations. Solution NMR of this toxin indicated a conformational heterogeneity with the existence of different conformers in solution, at slow and intermediate exchange rates relative to the NMR chemical shift time scale, similar to that reported for alpha-GI and alpha-MI. NMR structures were calculated for the major NMR signals representing more than 80% of the population at 5 degrees C. |
==About this Structure== | ==About this Structure== | ||
| - | 1B45 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_consors Conus consors] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1B45 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_consors Conus consors] 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=1B45 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Conus consors]] | [[Category: Conus consors]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bobenrieth, M | + | [[Category: Bobenrieth, M J.]] |
[[Category: Bouet, F.]] | [[Category: Bouet, F.]] | ||
[[Category: Favreau, P.]] | [[Category: Favreau, P.]] | ||
| - | [[Category: Gall, F | + | [[Category: Gall, F Le.]] |
[[Category: Krimm, I.]] | [[Category: Krimm, I.]] | ||
[[Category: Lamthanh, H.]] | [[Category: Lamthanh, H.]] | ||
| - | [[Category: Lancelin, J | + | [[Category: Lancelin, J M.]] |
[[Category: Letourneux, Y.]] | [[Category: Letourneux, Y.]] | ||
[[Category: Menez, A.]] | [[Category: Menez, A.]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:14 2008'' |
Revision as of 09:51, 21 February 2008
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ALPHA-CNIA CONOTOXIN FROM CONUS CONSORS, NMR, 43 STRUCTURES
Overview
Two novel alpha-conotoxins were purified and characterized from the venom of the fish-hunting cone snail Conus consors. These peptides were identified by screening HPLC fractions of the crude venom and by binding experiments with Torpedo nicotinic acetylcholine receptor. The toxins named alpha-CnIA and alpha-CnIB exhibited sequences of 14 and 12 amino acids, respectively. The alpha-CnIA represents the main alpha-conotoxin contained in the venom, whereas alpha-CnIB is present in a relatively small amount. Chemical synthesis of alpha-CnIA was carried out using the Fmoc methodology by selective disulfide bond formation. The biological activity of the toxin was assessed in fish and mice. The alpha-CnIA inhibited the fixation of iodinated alpha-bungarotoxin to Torpedo nicotinic acetylcholine receptors with an IC50 of 0.19 microM which can be compared to the IC50 of 0.31 microM found for the previously characterized alpha-MI isolated from the piscivorous Conus magus. The synthetic alpha-CnIA blocked spontaneous and evoked synaptic potentials in frog and mouse isolated neuromuscular preparations at sub-micromolar concentrations. Solution NMR of this toxin indicated a conformational heterogeneity with the existence of different conformers in solution, at slow and intermediate exchange rates relative to the NMR chemical shift time scale, similar to that reported for alpha-GI and alpha-MI. NMR structures were calculated for the major NMR signals representing more than 80% of the population at 5 degrees C.
About this Structure
1B45 is a Single protein structure of sequence from Conus consors with as ligand. Full crystallographic information is available from OCA.
Reference
Biochemical characterization and nuclear magnetic resonance structure of novel alpha-conotoxins isolated from the venom of Conus consors., Favreau P, Krimm I, Le Gall F, Bobenrieth MJ, Lamthanh H, Bouet F, Servent D, Molgo J, Menez A, Letourneux Y, Lancelin JM, Biochemistry. 1999 May 11;38(19):6317-26. PMID:10320362
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