|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution Structure of CssII== | | ==Solution Structure of CssII== |
| - | <StructureSection load='2li7' size='340' side='right'caption='[[2li7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2li7' size='340' side='right'caption='[[2li7]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[2li7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Centruroides_suffusus_suffusus Centruroides suffusus suffusus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LI7 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2li7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Centruroides_suffusus_suffusus Centruroides suffusus suffusus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LI7 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2li7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2li7 OCA], [https://pdbe.org/2li7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2li7 RCSB], [https://www.ebi.ac.uk/pdbsum/2li7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2li7 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2li7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2li7 OCA], [https://pdbe.org/2li7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2li7 RCSB], [https://www.ebi.ac.uk/pdbsum/2li7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2li7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SCX2_CENSU SCX2_CENSU]] Beta toxin. Both native and non-amidated recombinant forms of this protein bind in a voltage-independent fashion at site-4 of Nav1.6/SCN8A voltage-gated sodium channels. This binding shifts the voltage of activation towards more negative potentials which in turn affects sodium channel activation and promotes spontaneous and repetitive firing. This toxin is only active against mammals. Binds to phospholipids.<ref>PMID:17544584</ref> <ref>PMID:2435711</ref>
| + | [https://www.uniprot.org/uniprot/SCX2_CENSU SCX2_CENSU] Beta toxin. Both native and non-amidated recombinant forms of this protein bind in a voltage-independent fashion at site-4 of Nav1.6/SCN8A voltage-gated sodium channels. This binding shifts the voltage of activation towards more negative potentials which in turn affects sodium channel activation and promotes spontaneous and repetitive firing. This toxin is only active against mammals. Binds to phospholipids.<ref>PMID:17544584</ref> <ref>PMID:2435711</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 25: |
| | [[Category: Centruroides suffusus suffusus]] | | [[Category: Centruroides suffusus suffusus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Corzo, G]] | + | [[Category: Corzo G]] |
| - | [[Category: Delepierre, M]] | + | [[Category: Delepierre M]] |
| - | [[Category: Possani, L D]] | + | [[Category: Possani LD]] |
| - | [[Category: Rio-Portilla, F del]]
| + | [[Category: Saucedo AL]] |
| - | [[Category: Saucedo, A L]] | + | [[Category: Del Rio-Portilla F]] |
| - | [[Category: Alfa beta scorpion toxin]] | + | |
| - | [[Category: Cssii]]
| + | |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
SCX2_CENSU Beta toxin. Both native and non-amidated recombinant forms of this protein bind in a voltage-independent fashion at site-4 of Nav1.6/SCN8A voltage-gated sodium channels. This binding shifts the voltage of activation towards more negative potentials which in turn affects sodium channel activation and promotes spontaneous and repetitive firing. This toxin is only active against mammals. Binds to phospholipids.[1] [2]
Publication Abstract from PubMed
The three-dimensional structures of the long-chain mammalian scorpion beta-toxin CssII from Centruroides suffusus suffusus and of its recombinant form, HisrCssII, were determined by NMR. The neurotoxin CssII (nCssII) is a 66 amino acid long peptide with four disulfide bridges; it is the most abundant and deadly toxin from the venom of this scorpion. Both native and recombinant CssII structures were determined by nuclear magnetic resonance using a total of 828 sequential distance constraints derived from the volume integration of the cross peaks observed in 2D NOESY spectra. Both nCssII and HisrCssII structures display a mixed alpha/beta fold stabilized by four disulfide bridges formed between pairs of cysteines: C1-C8, C2-C5, C3-C6, and C4-C7 (the numbers indicate the relative positions of the cysteine residues in the primary structure), with a distortion induced by two cis-prolines in its C-terminal part. The native CssII electrostatic surface was compared to both the recombinant one and to the Cn2 toxin, from the scorpion Centruroides noxius, which is also toxic to mammals. Structural features such N- and C-terminal differences could influence toxin specificity and affinity towards isoforms of different sub-types of Na(v) channels.
Solution structure of native and recombinant expressed toxin CssII from the venom of the scorpion Centruroides suffusus suffusus, and their effects on Nav1.5 Sodium channels.,Saucedo AL, Del Rio-Portilla F, Picco C, Estrada G, Prestipino G, Possani LD, Delepierre M, Corzo G Biochim Biophys Acta. 2012 Mar;1824(3):478-87. Epub 2012 Jan 11. PMID:22251893[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Estrada G, Garcia BI, Schiavon E, Ortiz E, Cestele S, Wanke E, Possani LD, Corzo G. Four disulfide-bridged scorpion beta neurotoxin CssII: heterologous expression and proper folding in vitro. Biochim Biophys Acta. 2007 Aug;1770(8):1161-8. Epub 2007 May 1. PMID:17544584 doi:http://dx.doi.org/10.1016/j.bbagen.2007.04.006
- ↑ Martin MF, Garcia y Perez LG, el Ayeb M, Kopeyan C, Bechis G, Jover E, Rochat H. Purification and chemical and biological characterizations of seven toxins from the Mexican scorpion, Centruroides suffusus suffusus. J Biol Chem. 1987 Apr 5;262(10):4452-9. PMID:2435711
- ↑ Saucedo AL, Del Rio-Portilla F, Picco C, Estrada G, Prestipino G, Possani LD, Delepierre M, Corzo G. Solution structure of native and recombinant expressed toxin CssII from the venom of the scorpion Centruroides suffusus suffusus, and their effects on Nav1.5 Sodium channels. Biochim Biophys Acta. 2012 Mar;1824(3):478-87. Epub 2012 Jan 11. PMID:22251893 doi:10.1016/j.bbapap.2012.01.003
|
