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| | ==Solution Structure of a Short-chain LaIT1 from the Venom of Scorpion Liocheles australasiae== | | ==Solution Structure of a Short-chain LaIT1 from the Venom of Scorpion Liocheles australasiae== |
| - | <StructureSection load='2lds' size='340' side='right'caption='[[2lds]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2lds' size='340' side='right'caption='[[2lds]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lds]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dwarf_wood_scorpion Dwarf wood scorpion]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2LDS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lds]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Liocheles_australasiae Liocheles australasiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LDS FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2lds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lds OCA], [http://pdbe.org/2lds PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lds RCSB], [http://www.ebi.ac.uk/pdbsum/2lds PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lds 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=2lds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lds OCA], [https://pdbe.org/2lds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lds RCSB], [https://www.ebi.ac.uk/pdbsum/2lds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lds ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LAIT1_LIOAU LAIT1_LIOAU]] Affects the activity of both ryanodine-sensitive calcium-release channels RyR1 and RyR2 with high potency. At lower concentrations the toxin increases full openings of the RyRs, and at higher concentrations it inhibits full openings and induce openings to subconductance levels and reduces the number of full conductance openings. The different actions may be attributed to the toxins binding at different sites on the RyRs, with binding at a high-affinity site mediating the increase in full openings and the induction of subconductance states evoked upon binding to a lower-affinity site (By similarity). Shows insect lethality against crickets and common cutworms (only shows paralysis against cockroaches), but no toxicity is observed in mice.<ref>PMID:17681581</ref> <ref>PMID:21782787</ref> | + | [https://www.uniprot.org/uniprot/LAIT1_LIOAU LAIT1_LIOAU] Affects the activity of both ryanodine-sensitive calcium-release channels RyR1 and RyR2 with high potency. At lower concentrations the toxin increases full openings of the RyRs, and at higher concentrations it inhibits full openings and induce openings to subconductance levels and reduces the number of full conductance openings. The different actions may be attributed to the toxins binding at different sites on the RyRs, with binding at a high-affinity site mediating the increase in full openings and the induction of subconductance states evoked upon binding to a lower-affinity site (By similarity). Shows insect lethality against crickets and common cutworms (only shows paralysis against cockroaches), but no toxicity is observed in mice.<ref>PMID:17681581</ref> <ref>PMID:21782787</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dwarf wood scorpion]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Horita, S]] | + | [[Category: Liocheles australasiae]] |
| - | [[Category: Miyakawa, T]] | + | [[Category: Horita S]] |
| - | [[Category: Nagata, K]] | + | [[Category: Miyakawa T]] |
| - | [[Category: Tanokura, M]] | + | [[Category: Nagata K]] |
| - | [[Category: Scorpion toxin]]
| + | [[Category: Tanokura M]] |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
LAIT1_LIOAU Affects the activity of both ryanodine-sensitive calcium-release channels RyR1 and RyR2 with high potency. At lower concentrations the toxin increases full openings of the RyRs, and at higher concentrations it inhibits full openings and induce openings to subconductance levels and reduces the number of full conductance openings. The different actions may be attributed to the toxins binding at different sites on the RyRs, with binding at a high-affinity site mediating the increase in full openings and the induction of subconductance states evoked upon binding to a lower-affinity site (By similarity). Shows insect lethality against crickets and common cutworms (only shows paralysis against cockroaches), but no toxicity is observed in mice.[1] [2]
Publication Abstract from PubMed
The solution structure of an insecticidal toxin LaIT1, a 36-residue peptide with a unique amino-acid sequence and two disulfide bonds, isolated from the venom of the scorpion Liocheles australasiae was determined by heteronuclear NMR spectroscopy. Structural similarity search showed that LaIT1 exhibits an inhibitory cystine knot (ICK)-like fold, which usually contains three or more disulfide bonds. Mutational analysis has revealed that two Arg residues of LaIT1, Arg(13) and Arg(15), play significant roles in insecticidal activity.
Solution structure of a short-chain insecticidal toxin LaIT1 from the venom of scorpion Liocheles australasiae.,Horita S, Matsushita N, Kawachi T, Ayabe R, Miyashita M, Miyakawa T, Nakagawa Y, Nagata K, Miyagawa H, Tanokura M Biochem Biophys Res Commun. 2011 Aug 12;411(4):738-44. Epub 2011 Jul 18. PMID:21782787[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matsushita N, Miyashita M, Sakai A, Nakagawa Y, Miyagawa H. Purification and characterization of a novel short-chain insecticidal toxin with two disulfide bridges from the venom of the scorpion Liocheles australasiae. Toxicon. 2007 Nov;50(6):861-7. Epub 2007 Jun 26. PMID:17681581 doi:http://dx.doi.org/10.1016/j.toxicon.2007.06.014
- ↑ Horita S, Matsushita N, Kawachi T, Ayabe R, Miyashita M, Miyakawa T, Nakagawa Y, Nagata K, Miyagawa H, Tanokura M. Solution structure of a short-chain insecticidal toxin LaIT1 from the venom of scorpion Liocheles australasiae. Biochem Biophys Res Commun. 2011 Aug 12;411(4):738-44. Epub 2011 Jul 18. PMID:21782787 doi:10.1016/j.bbrc.2011.07.016
- ↑ Horita S, Matsushita N, Kawachi T, Ayabe R, Miyashita M, Miyakawa T, Nakagawa Y, Nagata K, Miyagawa H, Tanokura M. Solution structure of a short-chain insecticidal toxin LaIT1 from the venom of scorpion Liocheles australasiae. Biochem Biophys Res Commun. 2011 Aug 12;411(4):738-44. Epub 2011 Jul 18. PMID:21782787 doi:10.1016/j.bbrc.2011.07.016
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