2lds: Difference between revisions
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[[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> | [[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> | <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> | ||
<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lds OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lds RCSB], [http://www.ebi.ac.uk/pdbsum/2lds PDBsum]</span><br> | |||
== Publication Abstract from PubMed == | == 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. | 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. | ||