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Solution structure of a short-chain insecticidal toxin LaIT1 from the venom of scorpion Liocheles australasiae

Solution structure of a short-chain insecticidal toxin LaIT1 from the venom of scorpion Liocheles australasiae,10.1016/j.bbrc.2011.07.016,Biochemical

Solution structure of a short-chain insecticidal toxin LaIT1 from the venom of scorpion Liocheles australasiae  
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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, Arg13 and Arg15, play significant roles in insecticidal activity.
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