Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Japan.
Biochem Biophys Res Commun. 2011 Aug 12;411(4):738-44. doi: 10.1016/j.bbrc.2011.07.016. Epub 2011 Jul 18.
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.
从澳大利亚蝎子毒液中分离得到的一种 36 个氨基酸残基的具有独特氨基酸序列和两个二硫键的杀虫毒素 LaIT1 的溶液结构通过异核 NMR 光谱法确定。结构相似性搜索表明,LaIT1 具有抑制半胱氨酸结(ICK)样折叠,通常包含三个或更多的二硫键。突变分析表明,LaIT1 的两个精氨酸残基 Arg(13)和 Arg(15)在杀虫活性中起重要作用。