2LDS

Solution Structure of a Short-chain LaIT1 from the Venom of Scorpion Liocheles australasiae

Summary for 2LDS

• Entry DOI: 10.2210/pdb2lds/pdb
• NMR Information: BMRB: 17681
• Descriptor: Insecticidal toxin LaIT1 (1 entity in total)
• Functional Keywords: inhibitor cystine knot (ick) fold, scorpion toxin, toxin
• Biological source: Liocheles australasiae (Wood scorpion)
• Cellular location: Secreted: P0C5F2
• Total number of polymer chains: 1
• Total formula weight: 4214.99

Authors

Horita, S.,Miyakawa, T.,Nagata, K.,Tanokura, M. (deposition date: 2011-06-01, release date: 2011-09-14, Last modification date: 2024-10-30)

Primary citation

Horita, S.,Matsushita, N.,Kawachi, T.,Ayabe, R.,Miyashita, M.,Miyakawa, T.,Nakagawa, Y.,Nagata, K.,Miyagawa, H.,Tanokura, M.
Solution structure of a short-chain insecticidal toxin LaIT1 from the venom of scorpion Liocheles australasiae.
Biochem.Biophys.Res.Commun., 411:738-744, 2011

PubMed 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.

PubMed: 21782787
DOI: 10.1016/j.bbrc.2011.07.016

Experimental method

SOLUTION NMR