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

Biochemical and Biophysical Research Communications, Vol.411, No.4, 738-744, 2011

DOI10.1016/j.bbrc.2011.07.016 Export Citation

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

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. (C) 2011 Elsevier Inc. All rights reserved.

Keywords:Inhibitory cystine knot fold;LaIT1;Nuclear magnetic resonance;Scorpion toxin;Solution structure