2lds
From Proteopedia
Solution Structure of a Short-chain LaIT1 from the Venom of Scorpion Liocheles australasiae
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 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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