1dl0

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Revision as of 12:02, 11 September 2015

SOLUTION STRUCTURE OF THE INSECTICIDAL NEUROTOXIN J-ATRACOTOXIN-HV1C

Structural highlights

1dl0 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[TK1C_HADVE] This excitatory toxin inhibits insect calcium-activated potassium (KCa) channels (Slo-type). Pan-neuronal expression in Drosophila is lethal but flies engineered to express the toxin only in clock neurons have defects in circadian rhythm but a normal lifespan.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

We have isolated a family of insect-selective neurotoxins from the venom of the Australian funnel-web spider that appear to be good candidates for biopesticide engineering. These peptides, which we have named the Janus-faced atracotoxins (J-ACTXs), each contain 36 or 37 residues, with four disulfide bridges, and they show no homology to any sequences in the protein/DNA databases. The three-dimensional structure of one of these toxins reveals an extremely rare vicinal disulfide bridge that we demonstrate to be critical for insecticidal activity. We propose that J-ACTX comprises an ancestral protein fold that we refer to as the disulfide-directed beta-hairpin.

Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge.,Wang X, Connor M, Smith R, Maciejewski MW, Howden ME, Nicholson GM, Christie MJ, King GF Nat Struct Biol. 2000 Jun;7(6):505-13. PMID:10881200^[5]

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

References

↑ Wang X, Connor M, Smith R, Maciejewski MW, Howden ME, Nicholson GM, Christie MJ, King GF. Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge. Nat Struct Biol. 2000 Jun;7(6):505-13. PMID:10881200 doi:http://dx.doi.org/10.1038/75921
↑ Tedford HW, Maggio F, Reenan RA, King G. A model genetic system for testing the in vivo function of peptide toxins. Peptides. 2007 Jan;28(1):51-6. Epub 2006 Dec 1. PMID:17141372 doi:http://dx.doi.org/10.1016/j.peptides.2006.08.026
↑ Gunning SJ, Maggio F, Windley MJ, Valenzuela SM, King GF, Nicholson GM. The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels. FEBS J. 2008 Aug;275(16):4045-59. doi: 10.1111/j.1742-4658.2008.06545.x. Epub, 2008 Jul 9. PMID:18625007 doi:http://dx.doi.org/10.1111/j.1742-4658.2008.06545.x
↑ Wu Y, Cao G, Pavlicek B, Luo X, Nitabach MN. Phase coupling of a circadian neuropeptide with rest/activity rhythms detected using a membrane-tethered spider toxin. PLoS Biol. 2008 Nov 4;6(11):e273. doi: 10.1371/journal.pbio.0060273. PMID:18986214 doi:http://dx.doi.org/10.1371/journal.pbio.0060273
↑ Wang X, Connor M, Smith R, Maciejewski MW, Howden ME, Nicholson GM, Christie MJ, King GF. Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge. Nat Struct Biol. 2000 Jun;7(6):505-13. PMID:10881200 doi:http://dx.doi.org/10.1038/75921

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dl0"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1dl0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DL0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DL0 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=1dl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dl0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dl0 RCSB], [http://www.ebi.ac.uk/pdbsum/1dl0 PDBsum]</span></td></tr>
+</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=1dl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dl0 OCA], [http://pdbe.org/1dl0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dl0 RCSB], [http://www.ebi.ac.uk/pdbsum/1dl0 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TJT1C_HADVE TJT1C_HADVE]] This excitatory toxin inhibits insect calcium-activated potassium (KCa) channels (Slo-type). Pan-neuronal expression in Drosophila is lethal but flies engineered to express the toxin only in clock neurons have defects in circadian rhythm but a normal lifespan.<ref>PMID:10881200</ref> <ref>PMID:17141372</ref> <ref>PMID:18625007</ref> <ref>PMID:18986214</ref>
+[[http://www.uniprot.org/uniprot/TK1C_HADVE TK1C_HADVE]] This excitatory toxin inhibits insect calcium-activated potassium (KCa) channels (Slo-type). Pan-neuronal expression in Drosophila is lethal but flies engineered to express the toxin only in clock neurons have defects in circadian rhythm but a normal lifespan.<ref>PMID:10881200</ref> <ref>PMID:17141372</ref> <ref>PMID:18625007</ref> <ref>PMID:18986214</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 15: / Line 15: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1dl0" style="background-color:#fffaf0;"></div>
 ==See Also==

1dl0

From Proteopedia

Revision as of 12:02, 11 September 2015

SOLUTION STRUCTURE OF THE INSECTICIDAL NEUROTOXIN J-ATRACOTOXIN-HV1C

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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