1b3c

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[[Image:1b3c.gif|left|200px]]
 
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==SOLUTION STRUCTURE OF A BETA-NEUROTOXIN FROM THE NEW WORLD SCORPION CENTRUROIDES SCULPTURATUS EWING==
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The line below this paragraph, containing "STRUCTURE_1b3c", creates the "Structure Box" on the page.
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<StructureSection load='1b3c' size='340' side='right'caption='[[1b3c]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1b3c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Centruroides_sculpturatus Centruroides sculpturatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B3C FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 40 models</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b3c OCA], [https://pdbe.org/1b3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b3c RCSB], [https://www.ebi.ac.uk/pdbsum/1b3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b3c ProSAT]</span></td></tr>
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{{STRUCTURE_1b3c| PDB=1b3c | SCENE= }}
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</table>
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== Function ==
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'''SOLUTION STRUCTURE OF A BETA-NEUROTOXIN FROM THE NEW WORLD SCORPION CENTRUROIDES SCULPTURATUS EWING'''
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[https://www.uniprot.org/uniprot/SCXI_CENSC SCXI_CENSC] Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. Affects channels from chicken and frog.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/1b3c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1b3c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
We report the detailed solution structure of the 7.2 kDa protein CsE-I, a beta-neurotoxin from the New World scorpion Centruroides sculpturatus Ewing. This toxin binds to sodium channels, but unlike the alpha-neurotoxins, shifts the voltage of activation toward more negative potentials causing the membrane to fire spontaneously. Sequence-specific proton NMR assignments were made using 600 MHz 2D-NMR data. Distance geometry and dynamical simulated annealing refinements were performed using experimental distance and torsion angle constraints from NOESY and pH-COSY data. A family of 40 structures without constraint violations was generated, and an energy-minimized average structure was computed. The backbone conformation of the CsE-I toxin shows similar secondary structural features as the prototypical alpha-neurotoxin, CsE-v3, and is characterized by a short 2(1/2)-turn alpha-helix and a 3-strand antiparallel beta-sheet, both held together by disulfide bridges. The RMSD for the backbone atoms between CsE-I and CsE-v3 is 1.48 A. Despite this similarity in the overall backbone folding, the these two proteins show some important differences in the primary structure (sequence) and electrostatic potential surfaces. Our studies provide a basis for unravelling the role of these differences in relation to the known differences in the receptor sites on the voltage sensitive sodium channel for the alpha- and beta-neurotoxins.
We report the detailed solution structure of the 7.2 kDa protein CsE-I, a beta-neurotoxin from the New World scorpion Centruroides sculpturatus Ewing. This toxin binds to sodium channels, but unlike the alpha-neurotoxins, shifts the voltage of activation toward more negative potentials causing the membrane to fire spontaneously. Sequence-specific proton NMR assignments were made using 600 MHz 2D-NMR data. Distance geometry and dynamical simulated annealing refinements were performed using experimental distance and torsion angle constraints from NOESY and pH-COSY data. A family of 40 structures without constraint violations was generated, and an energy-minimized average structure was computed. The backbone conformation of the CsE-I toxin shows similar secondary structural features as the prototypical alpha-neurotoxin, CsE-v3, and is characterized by a short 2(1/2)-turn alpha-helix and a 3-strand antiparallel beta-sheet, both held together by disulfide bridges. The RMSD for the backbone atoms between CsE-I and CsE-v3 is 1.48 A. Despite this similarity in the overall backbone folding, the these two proteins show some important differences in the primary structure (sequence) and electrostatic potential surfaces. Our studies provide a basis for unravelling the role of these differences in relation to the known differences in the receptor sites on the voltage sensitive sodium channel for the alpha- and beta-neurotoxins.
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==About this Structure==
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Solution structure of a beta-neurotoxin from the New World scorpion Centruroides sculpturatus Ewing.,Jablonsky MJ, Jackson PL, Trent JO, Watt DD, Krishna NR Biochem Biophys Res Commun. 1999 Jan 19;254(2):406-12. PMID:9918851<ref>PMID:9918851</ref>
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1B3C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Centruroides_sculpturatus Centruroides sculpturatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B3C OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Solution structure of a beta-neurotoxin from the New World scorpion Centruroides sculpturatus Ewing., Jablonsky MJ, Jackson PL, Trent JO, Watt DD, Krishna NR, Biochem Biophys Res Commun. 1999 Jan 19;254(2):406-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9918851 9918851]
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</div>
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<div class="pdbe-citations 1b3c" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Centruroides sculpturatus]]
[[Category: Centruroides sculpturatus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Jablonsky, M J.]]
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[[Category: Jablonsky MJ]]
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[[Category: Jackson, P L.]]
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[[Category: Jackson PL]]
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[[Category: Krishna, N R.]]
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[[Category: Krishna NR]]
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[[Category: Trent, J O.]]
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[[Category: Trent JO]]
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[[Category: Watt, D D.]]
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[[Category: Watt DD]]
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[[Category: New world toxin]]
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[[Category: Scorpion neurotoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:00:33 2008''
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Current revision

SOLUTION STRUCTURE OF A BETA-NEUROTOXIN FROM THE NEW WORLD SCORPION CENTRUROIDES SCULPTURATUS EWING

PDB ID 1b3c

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