View source for 1ptx


==CRYSTAL STRUCTURE OF TOXIN II FROM THE SCORPION ANDROCTONUS AUSTRALIS HECTOR REFINED AT 1.3 ANGSTROMS RESOLUTION==
<StructureSection load='1ptx' size='340' side='right'caption='[[1ptx]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ptx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Androctonus_australis Androctonus australis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PTX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</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=1ptx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ptx OCA], [https://pdbe.org/1ptx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ptx RCSB], [https://www.ebi.ac.uk/pdbsum/1ptx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ptx ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/SCX2_ANDAU SCX2_ANDAU] Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active against mammals.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pt/1ptx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1ptx ConSurf].
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== Publication Abstract from PubMed ==
The crystal structure of toxin II from the scorpion Androctonus australis Hector has been refined at 1.3 A resolution using restrained least-squares methods. The final R-factor is 0.148 for the 13,619 reflections between 7.0 A and 1.3 A resolution with F &gt; 2.5 sigma (F) and the bond length standard deviation from ideality is 0.017 A. Although minor changes have been introduced relative to the model previously refined at 1.8 A resolution, the use of higher-resolution data has allowed the modelling of some discrete disorder. Thus, three residues (including a disulphide bridge) have been built with multiple conformations. Occupancies were refined for the 106 solvent molecules included in the model, nine of them with explicit multiple sites. There is well-defined electron density for some of the protein hydrogen atoms in the final difference Fourier map. A detailed description of the toxin structure is presented, along with a comparison with the high-resolution structure of the related variant-3 scorpion toxin.

Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 A resolution.,Housset D, Habersetzer-Rochat C, Astier JP, Fontecilla-Camps JC J Mol Biol. 1994 Apr 22;238(1):88-103. PMID:8145259<ref>PMID:8145259</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Androctonus australis]]
[[Category: Large Structures]]
[[Category: Fontecilla-Camps JC]]
[[Category: Housset D]]