Tracing protein evolution through ancestral structures of fish galectin

Ayumu Konno, Atsushi Kitagawa, Mizuki Watanabe, Tomohisa Ogawa, Tsuyoshi Shirai

    研究成果: Article査読

    11 被引用数 (Scopus)

    抄録

    Ancestral structures of fish galectins (congerins) were determined. The extant isoforms I and II of congerin are the components of a fish biological defense system and have rapidly differentiated under natural selection pressure, by which congerin I has experienced a protein-fold evolution. The dimer structure of the ancestral congerin demonstrated intermediate features of the extant isoforms. The protein-fold evolution was not observed in the ancestral structure, indicating it specifically occurred in congerin I lineage. Details of hydrogen bonding pattern at the dimer interface and the carbohydrate-binding site of the ancestor were different from the current proteins. The differences implied these proteins were under selection pressure for stabilizing dimer structure and differentiation in carbohydrate specificity. The ancestor had rather low cytotoxic activity than offspring, indicating selection was made to enhance this activity of congerins. Combined with functional analyses, the structure revealed atomic details of the differentiation process of the proteins.

    本文言語English
    ページ(範囲)711-721
    ページ数11
    ジャーナルStructure
    19
    5
    DOI
    出版ステータスPublished - 2011 5月 11

    ASJC Scopus subject areas

    • 構造生物学
    • 分子生物学

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