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1npi

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Tityus Serrulatus Neurotoxin (Ts1) at atomic resolution

Structural highlights

1npi is a 1 chain structure with sequence from Tityus serrulatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.16Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SCX1_TITSE 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. In addition, it stimulates the release of NO, IL-6 and TNF-alpha in J774.1 cells (PubMed:21549737). This toxin is active against both mammals and insects.^[1]

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 structure of the Ts1 toxin from the Brazilian scorpion Tityus serrulatus was investigated at atomic resolution using X-ray crystallography. Several positively charged niches exist on the Ts1 molecular surface, two of which were found to coordinate phosphate ions present in the crystallization solution. One phosphate ion is bound to the conserved basic Lys1 residue at the Ts1 N-terminus and to residue Asn49. The second ion was found to be caged by residues Lys12, Trp54 and Arg56. Lys12 and Tyr/Trp54 residues are strictly conserved in all classical scorpion beta-neurotoxins. The cavity formed by these residues may represent a special scaffold required for interaction between beta-neurotoxins and sodium channels. The charge distribution on the Ts1 surface and the results of earlier chemical modification studies and side-directed mutagenesis experiments strongly indicate that the phosphate-ion positions mark plausible binding sites to the Na(+) channel. The existence of two distinct binding sites on the Ts1 molecular surface provides an explanation for the competition between Ts1, depressant (LqhIT2) and excitatory (AaHIT) neurotoxins.

Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with Na+ channels.,Pinheiro CB, Marangoni S, Toyama MH, Polikarpov I Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):405-15. Epub 2003, Feb 21. PMID:12595696^[2]

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

References

↑ Zoccal KF, Bitencourt Cda S, Secatto A, Sorgi CA, Bordon Kde C, Sampaio SV, Arantes EC, Faccioli LH. Tityus serrulatus venom and toxins Ts1, Ts2 and Ts6 induce macrophage activation and production of immune mediators. Toxicon. 2011 Jun;57(7-8):1101-8. doi: 10.1016/j.toxicon.2011.04.017. Epub 2011, Apr 29. PMID:21549737 doi:http://dx.doi.org/10.1016/j.toxicon.2011.04.017
↑ Pinheiro CB, Marangoni S, Toyama MH, Polikarpov I. Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with Na+ channels. Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):405-15. Epub 2003, Feb 21. PMID:12595696

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1npi' size='340' side='right'caption='[[1npi]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1npi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Tityus_serrulatus Tityus serrulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NPI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1npi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tityus_serrulatus Tityus serrulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NPI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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]] 1.16&#8491;</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=1npi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1npi OCA], [http://pdbe.org/1npi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1npi RCSB], [http://www.ebi.ac.uk/pdbsum/1npi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1npi ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1npi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1npi OCA], [https://pdbe.org/1npi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1npi RCSB], [https://www.ebi.ac.uk/pdbsum/1npi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1npi ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SCX1_TITSE SCX1_TITSE]] 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. In addition, it stimulates the release of NO, IL-6 and TNF-alpha in J774.1 cells (PubMed:21549737). This toxin is active against both mammals and insects.<ref>PMID:21549737</ref>
+[https://www.uniprot.org/uniprot/SCX1_TITSE SCX1_TITSE] 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. In addition, it stimulates the release of NO, IL-6 and TNF-alpha in J774.1 cells (PubMed:21549737). This toxin is active against both mammals and insects.<ref>PMID:21549737</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 35: @@
 [[Category: Large Structures]]
 [[Category: Tityus serrulatus]]
-[[Category: Marangoni, S]]
+[[Category: Marangoni S]]
-[[Category: Pinheiro, C B]]
+[[Category: Pinheiro CB]]
-[[Category: Polikarpov, I]]
+[[Category: Polikarpov I]]
-[[Category: Toyama, M H]]
+[[Category: Toyama MH]]
-[[Category: Toxin]]
-[[Category: Xcitatory neurotoxin]]

1npi

From Proteopedia

Current revision

Tityus Serrulatus Neurotoxin (Ts1) at atomic resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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