1v91

From Proteopedia

(Difference between revisions)

Revision as of 08:32, 10 September 2015

Solution structure of insectidal toxin delta-paluIT2-NH2

Structural highlights

1v91 is a 1 chain structure with sequence from Pireneitega luctuosa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1v90
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[TXDP2_PIRLC] Insecticidal toxin. Lethal to lepidopteran larvae. No adverse affects when intracerebroventricularly injected in mice at a dose of 0.2 ug but causes reversible paralysis of legs when injected intracerebroventricularly in mice at a dose of 2.0 ug. Binds to site 4 of insect voltage-gated sodium channel (Nav) and inhibits channel inactivation.^[1] ^[2]

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

Delta-paluIT1 and delta-paluIT2 are toxins purified from the venom of the spider Paracoelotes luctuosus. Similar in sequence to mu-agatoxins from Agelenopsis aperta, their pharmacological target is the voltage-gated insect sodium channel, of which they alter the inactivation properties in a way similar to alpha-scorpion toxins, but they bind on site 4 in a way similar to beta-scorpion toxins. We determined the solution structure of the two toxins by use of two-dimensional nuclear magnetic resonance (NMR) techniques followed by distance geometry and molecular dynamics. The structures of delta-paluIT1 and delta-paluIT2 belong to the inhibitory cystine knot structural family, i.e. a compact disulfide-bonded core from which four loops emerge. Delta-paluIT1 and delta-paluIT2 contain respectively two- and three-stranded anti-parallel beta-sheets as unique secondary structure. We compare the structure and the electrostatic anisotropy of those peptides to other sodium and calcium channel toxins, analyze the topological juxtaposition of key functional residues, and conclude that the recognition of insect voltage-gated sodium channels by these toxins involves the beta-sheet, in addition to loops I and IV. Besides the position of culprit residues on the molecular surface, difference in dipolar moment orientation is another determinant of receptor binding and biological activity differences. We also demonstrate by electrophysiological experiments on the cloned insect voltage-gated sodium channel, para, heterologuously co-expressed with the tipE subunit in Xenopus laevis oocytes, that delta-paluIT1 and delta-paluIT2 procure an increase of Na+ current. delta-PaluIT1-OH seems to have less effect when the same concentrations are used.

Solution structure of two insect-specific spider toxins and their pharmacological interaction with the insect voltage-gated Na+ channel.,Ferrat G, Bosmans F, Tytgat J, Pimentel C, Chagot B, Gilles N, Nakajima T, Darbon H, Corzo G Proteins. 2005 May 1;59(2):368-79. PMID:15726637^[3]

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

References

↑ Corzo G, Escoubas P, Stankiewicz M, Pelhate M, Kristensen CP, Nakajima T. Isolation, synthesis and pharmacological characterization of delta-palutoxins IT, novel insecticidal toxins from the spider Paracoelotes luctuosus (Amaurobiidae). Eur J Biochem. 2000 Sep;267(18):5783-95. PMID:10971590
↑ Corzo G, Escoubas P, Villegas E, Karbat I, Gordon D, Gurevitz M, Nakajima T, Gilles N. A spider toxin that induces a typical effect of scorpion alpha-toxins but competes with beta-toxins on binding to insect sodium channels. Biochemistry. 2005 Feb 8;44(5):1542-9. PMID:15683238 doi:http://dx.doi.org/10.1021/bi048434k
↑ Ferrat G, Bosmans F, Tytgat J, Pimentel C, Chagot B, Gilles N, Nakajima T, Darbon H, Corzo G. Solution structure of two insect-specific spider toxins and their pharmacological interaction with the insect voltage-gated Na+ channel. Proteins. 2005 May 1;59(2):368-79. PMID:15726637 doi:10.1002/prot.20424

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/1v91"

@@ Line 2: / Line 2: @@
 <StructureSection load='1v91' size='340' side='right' caption='[[1v91]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1v91]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoelotes_luctuosus Paracoelotes luctuosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V91 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V91 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1v91]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pireneitega_luctuosa Pireneitega luctuosa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V91 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V91 FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1v90|1v90]]</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=1v91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v91 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1v91 RCSB], [http://www.ebi.ac.uk/pdbsum/1v91 PDBsum]</span></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=1v91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v91 OCA], [http://pdbe.org/1v91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v91 RCSB], [http://www.ebi.ac.uk/pdbsum/1v91 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TXDP2_PARLU TXDP2_PARLU]] Insecticidal toxin. Lethal to lepidopteran larvae. No adverse affects when intracerebroventricularly injected in mice at a dose of 0.2 ug but causes reversible paralysis of legs when injected intracerebroventricularly in mice at a dose of 2.0 ug. Binds to site 4 of insect voltage-gated sodium channel (Nav) and inhibits channel inactivation.<ref>PMID:10971590</ref> <ref>PMID:15683238</ref>
+[[http://www.uniprot.org/uniprot/TXDP2_PIRLC TXDP2_PIRLC]] Insecticidal toxin. Lethal to lepidopteran larvae. No adverse affects when intracerebroventricularly injected in mice at a dose of 0.2 ug but causes reversible paralysis of legs when injected intracerebroventricularly in mice at a dose of 2.0 ug. Binds to site 4 of insect voltage-gated sodium channel (Nav) and inhibits channel inactivation.<ref>PMID:10971590</ref> <ref>PMID:15683238</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1v91" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Paracoelotes luctuosus]]
+[[Category: Pireneitega luctuosa]]
 [[Category: Bosmans, F]]
 [[Category: Chagot, B]]

1v91

From Proteopedia

Revision as of 08:32, 10 September 2015

Solution structure of insectidal toxin delta-paluIT2-NH2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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