1is3
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(New page: 200px<br /><applet load="1is3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1is3, resolution 1.45Å" /> '''LACTOSE AND MES-LIGA...)
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Revision as of 15:30, 20 November 2007
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LACTOSE AND MES-LIGANDED CONGERIN II
Overview
The crystal structure of congerin II, a galectin family lectin from conger, eel, was determined at 1.45A resolution. The previously determined, structure of its isoform, congerin I, had revealed a fold evolution via, strand swap; however, the structure of congerin II described here, resembles other prototype galectins. A comparison of the two congerin, genes with that of several other galectins suggests acceralated evolution, of both congerin genes following gene duplication. The presence of a Mes, (2-[N-morpholino]ethanesulfonic acid) molecule near the, carbohydrate-binding site in the crystal structure points to the, possibility of an additional binding site in congerin II. The binding site, consists of a group of residues that had been replaced following gene, duplication suggesting that the binding site was built under selective, pressure. Congerin II may be a protein specialized for biological defense, with an affinity for target carbohydrates on parasites' cell surface.
About this Structure
1IS3 is a Single protein structure of sequence from Conger myriaster with LAT and MES as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a conger eel galectin (congerin II) at 1.45A resolution: implication for the accelerated evolution of a new ligand-binding site following gene duplication., Shirai T, Matsui Y, Shionyu-Mitsuyama C, Yamane T, Kamiya H, Ishii C, Ogawa T, Muramoto K, J Mol Biol. 2002 Aug 30;321(5):879-89. PMID:12206768
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