2lds: Difference between revisions
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< | ==Solution Structure of a Short-chain LaIT1 from the Venom of Scorpion Liocheles australasiae== | ||
<StructureSection load='2lds' size='340' side='right'caption='[[2lds]]' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 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=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> | |||
== Function == | |||
[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;"> | |||
== 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<ref>PMID:21782787</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2lds" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Liocheles australasiae]] | [[Category: Liocheles australasiae]] | ||
[[Category: Horita | [[Category: Horita S]] | ||
[[Category: Miyakawa | [[Category: Miyakawa T]] | ||
[[Category: Nagata | [[Category: Nagata K]] | ||
[[Category: Tanokura | [[Category: Tanokura M]] | ||
Latest revision as of 11:17, 30 October 2024
Solution Structure of a Short-chain LaIT1 from the Venom of Scorpion Liocheles australasiaeSolution Structure of a Short-chain LaIT1 from the Venom of Scorpion Liocheles australasiae
Structural highlights
FunctionLAIT1_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 PubMedThe 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
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