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

研究成果: Article査読

32 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)879-889
ページ数11
ジャーナルJournal of Molecular Biology
321
5
DOI
出版ステータスPublished - 2002

ASJC Scopus subject areas

  • 構造生物学
  • 分子生物学

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