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[[ | ==Solution Structure of a Short-chain LaIT1 from the Venom of Scorpion Liocheles australasiae== | ||
<StructureSection load='2lds' size='340' side='right' caption='[[2lds]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |||
== Structural highlights == | |||
[[2lds]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Liocheles_australasiae Liocheles australasiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDS OCA]. <br> | |||
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | |||
== 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<ref>PMID:21782787</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== References == | |||
<references/> | |||
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</StructureSection> | |||
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[[Category: Liocheles australasiae]] | [[Category: Liocheles australasiae]] | ||
[[Category: Horita, S.]] | [[Category: Horita, S.]] | ||
Revision as of 11:26, 30 April 2014
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 highlights2lds 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 Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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