1b45: Difference between revisions

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[[Image:1b45.gif|left|200px]]<br /><applet load="1b45" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1b45.gif|left|200px]]<br /><applet load="1b45" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1b45" />

'''ALPHA-CNIA CONOTOXIN FROM CONUS CONSORS, NMR, 43 STRUCTURES'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1B45 OCA].

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==

Line 13:

[[Category: Conus consors]]

[[Category: Single protein]]

[[Category: Bobenrieth, M.J.]]

[[Category: Bobenrieth, M J.]]

[[Category: Bouet, F.]]

[[Category: Favreau, P.]]

[[Category: Gall, F.Le.]]

[[Category: Gall, F Le.]]

[[Category: Krimm, I.]]

[[Category: Lamthanh, H.]]

[[Category: Lancelin, J.M.]]

[[Category: Lancelin, J M.]]

[[Category: Letourneux, Y.]]

[[Category: Menez, A.]]

Line 30:

[[Category: toxin]]

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@@ Line 1: / Line 1: @@
-[[Image:1b45.gif|left|200px]]<br /><applet load="1b45" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1b45.gif|left|200px]]<br /><applet load="1b45" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1b45" />
 '''ALPHA-CNIA CONOTOXIN FROM CONUS CONSORS, NMR, 43 STRUCTURES'''<br />
 ==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.
+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==
-B45 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B45 OCA].
+B45 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==
@@ Line 13: / Line 13: @@
 [[Category: Conus consors]]
 [[Category: Single protein]]
-[[Category: Bobenrieth, M.J.]]
+[[Category: Bobenrieth, M J.]]
 [[Category: Bouet, F.]]
 [[Category: Favreau, P.]]
-[[Category: Gall, F.Le.]]
+[[Category: Gall, F Le.]]
 [[Category: Krimm, I.]]
 [[Category: Lamthanh, H.]]
-[[Category: Lancelin, J.M.]]
+[[Category: Lancelin, J M.]]
 [[Category: Letourneux, Y.]]
 [[Category: Menez, A.]]
@@ Line 30: / Line 30: @@
 [[Category: toxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:20:33 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:14 2008''