Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 321, Issue 5, Pages 879-889Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/S0022-2836(02)00700-3
Keywords
X-ray crystallography; galectin; protein fold; protein evolution; natural selection
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The crystal structure of congerin II, a galectin family lectin from conger eel, was determined at 1.45 Angstrom 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. (C) 2002 Elsevier Science Ltd. All rights reserved.
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