Ice-binding structure and mechanism of an antifreeze protein from winter flounder

F. Sicheri, D.S.C. Yang

    Research output: Contribution to journalArticleAcademicpeer-review

    305 Citations (Scopus)

    Abstract

    Antifreeze proteins provide fish with protection against the freezing effect of polar environments by binding to ice surfaces and inhibiting growth of ice crystals. We present the X-ray crystal structure at 1.5 Å resolution of a lone a-helical antifreeze protein from winter flounder, which provides a detailed look at its ice-binding features. These consist of four repeated ice-binding motifs, the side chains of which are inherently rigid or restrained by pairwise side-chain interactions to form a flat binding surface. Elaborate amino- and carboxy-terminal cap structures are also present, which explain the protein's rich a-helical content in solution. We propose an ice-binding model that accounts for the binding specificity of the antifreeze protein along the axes of the {2021} ice planes.
    Original languageEnglish
    Pages (from-to)427-431
    Number of pages5
    JournalNature
    Volume375
    DOIs
    Publication statusPublished - 1995

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    Antifreeze Proteins
    Flounder
    Ice
    Crystallization
    Freezing
    Fishes
    X-Rays

    Cite this

    Sicheri, F. ; Yang, D.S.C. / Ice-binding structure and mechanism of an antifreeze protein from winter flounder. In: Nature. 1995 ; Vol. 375. pp. 427-431.
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    Ice-binding structure and mechanism of an antifreeze protein from winter flounder. / Sicheri, F.; Yang, D.S.C.

    In: Nature, Vol. 375, 1995, p. 427-431.

    Research output: Contribution to journalArticleAcademicpeer-review

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