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1ptx

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Revision as of 10:48, 19 May 2021

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

Structural highlights

1ptx is a 1 chain structure with sequence from Andau. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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 > 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Housset D, Habersetzer-Rochat C, Astier JP, Fontecilla-Camps JC. Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 A resolution. J Mol Biol. 1994 Apr 22;238(1):88-103. PMID:8145259 doi:http://dx.doi.org/10.1006/jmbi.1994.1270

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ptx"

Categories: Andau | Large Structures | Fontecilla-Camps, J C | Housset, D | Toxin

@@ Line 3: / Line 3: @@
 <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 [http://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 [http://oca.weizmann.ac.il/oca-docs/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/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>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ptx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ptx OCA], [http://pdbe.org/1ptx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ptx RCSB], [http://www.ebi.ac.uk/pdbsum/1ptx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ptx ProSAT]</span></td></tr>
+</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>
 == Function ==
-[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 29: @@
 ==See Also==
-*[[Potassium channel toxin|Potassium channel toxin]]
+*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
 == References ==
 <references/>

1ptx

From Proteopedia

Revision as of 10:48, 19 May 2021

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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