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 α-helical antifreeze protein from winter flounder, which provides a detailed look at its icebinding features. These consist of four repeated ice-binding motifs, the side chains of which are inherently rigid or restrained by pair-wise 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 α-helical content in solution. We propose an ice-binding model that accounts for the binding specificity of the antifreeze protein along the <011¯2> axes of the {202¯1} ice planes1.
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Sicheri, F., Yang, D. Ice-binding structure and mechanism of an antifreeze protein from winter flounder. Nature 375, 427–431 (1995). https://doi.org/10.1038/375427a0
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DOI: https://doi.org/10.1038/375427a0
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