TY  - JOUR
PY  - 2011//
TI  - Solution structure of a short-chain insecticidal toxin LaIT1 from the venom of scorpion Liocheles australasiae
JO  - Biochemical and biophysical research communications
A1  - Horita, Shoichiro
A1  - Matsushita, Nobuto
A1  - Kawachi, Tomoyuki
A1  - Ayabe, Reed
A1  - Miyashita, Masahiro
A1  - Miyakawa, Takuya
A1  - Nakagawa, Yoshiaki
A1  - Nagata, Koji
A1  - Miyagawa, Hisashi
A1  - Tanokura, Masaru
SP  - 738
EP  - 744
VL  - 411
IS  - 4
N2  - 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>
LA  - en
SN  - 0006-291X
UR  - http://dx.doi.org/10.1016/j.bbrc.2011.07.016
ID  - ref1
ER  -