2lds

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

Structural highlights 2lds is a 1 chain structure with sequence from Liocheles australasiae. Full experimental information is available from OCA. Activity: Glucokinase, with EC number 2.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. 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 Biochem Biophys Res Commun. 2011 Aug 12;411(4):738-44. Epub 2011 Jul 18. PMID:21782787 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 2lds, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image