1is5
From Proteopedia
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'''Ligand free Congerin II''' | '''Ligand free Congerin II''' | ||
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[[Category: Shirai, T.]] | [[Category: Shirai, T.]] | ||
[[Category: Yamane, T.]] | [[Category: Yamane, T.]] | ||
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Revision as of 17:20, 2 May 2008
Ligand free 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
1IS5 is a Single protein structure of sequence from Conger myriaster. 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 Page seeded by OCA on Fri May 2 20:20:58 2008
