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== | ==SOLUTION STRUCTURE OF THE INSECTICIDAL NEUROTOXIN J-ATRACOTOXIN-HV1C== | ||
[[1dl0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DL0 OCA]. | <StructureSection load='1dl0' size='340' side='right'caption='[[1dl0]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1dl0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hadronyche_versuta Hadronyche versuta]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1DL0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1dl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dl0 OCA], [https://pdbe.org/1dl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dl0 RCSB], [https://www.ebi.ac.uk/pdbsum/1dl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dl0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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 == | |||
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<ref>PMID:10881200</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1dl0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Hadronyche versuta]] | ||
[[Category: Large Structures]] | |||
[[Category: King GF]] | |||
[[Category: Wang XH]] | |||
Latest revision as of 11:23, 6 November 2024
SOLUTION STRUCTURE OF THE INSECTICIDAL NEUROTOXIN J-ATRACOTOXIN-HV1CSOLUTION STRUCTURE OF THE INSECTICIDAL NEUROTOXIN J-ATRACOTOXIN-HV1C
Structural highlights
FunctionTK1C_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 PubMedWe 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
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