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

F. Sicheri, D.S.C. Yang

    Onderzoeksoutput: Bijdrage aan tijdschriftTijdschriftartikelAcademicpeer review

    309 Citaten (Scopus)

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    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.
    Originele taal-2Engels
    Pagina's (van-tot)427-431
    Aantal pagina's5
    TijdschriftNature
    Volume375
    DOI's
    StatusGepubliceerd - 1995

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