1ptx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='1ptx' size='340' side='right'caption='[[1ptx]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
<StructureSection load='1ptx' size='340' side='right'caption='[[1ptx]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1ptx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Andau Andau]. 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>
+
<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='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>
+
</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>
</table>
</table>
== Function ==
== 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.
+
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 18: Line 19:
</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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== 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>
 
-
</div>
 
-
<div class="pdbe-citations 1ptx" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Andau]]
+
[[Category: Androctonus australis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Fontecilla-Camps, J C]]
+
[[Category: Fontecilla-Camps JC]]
-
[[Category: Housset, D]]
+
[[Category: Housset D]]
-
[[Category: Toxin]]
+

Revision as of 05:59, 17 April 2024

CRYSTAL STRUCTURE OF TOXIN II FROM THE SCORPION ANDROCTONUS AUSTRALIS HECTOR REFINED AT 1.3 ANGSTROMS RESOLUTION

PDB ID 1ptx

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools