Crystal structure of a conger eel galectin (Congerin II) at 1.45 Å resolution: Implication for the accelerated evolution of a new ligand-binding site following gene duplication

Tsuyoshi Shirai, Yuuka Matsui, Clara Shionyu-Mitsuyama, Takashi Yamane, Hisao Kamiya, Chihiro Ishii, Tomohisa Ogawa, Koji Muramoto

    Research output: Contribution to journalArticlepeer-review

    35 Citations (Scopus)

    Abstract

    The crystal structure of congerin II, a galectin family lectin from conger eel, was determined at 1.45 Å 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.

    Original languageEnglish
    Pages (from-to)879-889
    Number of pages11
    JournalJournal of Molecular Biology
    Volume321
    Issue number5
    DOIs
    Publication statusPublished - 2002

    Keywords

    • Galectin
    • Natural selection
    • Protein evolution
    • Protein fold
    • X-ray crystallography

    ASJC Scopus subject areas

    • Structural Biology
    • Molecular Biology

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