This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1is6
From Proteopedia
|
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
1IS6 is a Single protein structure of sequence from Conger myriaster with MES as ligand. 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 Tue Nov 20 17:37:43 2007
