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    Structure of a Kunitz-type potato cathepsin D inhibitor

    Guo, J. and Erskine, Peter T. and Coker, A.R. and Wood, S.P. and Cooper, Jonathan B. (2015) Structure of a Kunitz-type potato cathepsin D inhibitor. Journal of Structural Biology 192 (3), pp. 554-560. ISSN 1047-8477.

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    Potato cathepsin D inhibitor (PDI) is a glycoprotein of 188 amino acids which can inhibit both the aspartic protease cathepsin D and the serine protease trypsin. Here we report the first X-ray structure of PDI at a resolution of 2.1 Å showing that PDI adopts a β-trefoil fold, which is typical of the Kunitz-family protease inhibitors, with the inhibitory loops protruding from the core. Possible reactive-site loops including one involving a unique disulphide and another involving a protruding 310 helix are identified and docking studies indicate the mode of action this unusual bi-functional inhibitor.


    Item Type: Article
    Additional Information: Corrigendum at
    Keyword(s) / Subject(s): Potato cathepsin D inhibitor, Kunitz-type protease inhibitor, Protein X-ray structure, Reactive-site loop, Docking
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Research Centres and Institutes: Birkbeck Knowledge Lab
    Depositing User: Administrator
    Date Deposited: 03 Nov 2015 17:54
    Last Modified: 02 Aug 2023 17:19


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