@article{ref1,
title="Solution structure of a short-chain insecticidal toxin LaIT1 from the venom of scorpion Liocheles australasiae",
journal="Biochemical and biophysical research communications",
year="2011",
author="Horita, Shoichiro and Matsushita, Nobuto and Kawachi, Tomoyuki and Ayabe, Reed and Miyashita, Masahiro and Miyakawa, Takuya and Nakagawa, Yoshiaki and Nagata, Koji and Miyagawa, Hisashi and Tanokura, Masaru",
volume="411",
number="4",
pages="738-744",
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.<p /> <p>Language: en</p>",
language="en",
issn="0006-291X",
doi="10.1016/j.bbrc.2011.07.016",
url="http://dx.doi.org/10.1016/j.bbrc.2011.07.016"
}