Citation

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; 411(4): 738-744.

Affiliation

Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.

Copyright

(Copyright © 2011, Academic Press)

DOI

10.1016/j.bbrc.2011.07.016

PMID

21782787

Abstract

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.

Language: en