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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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    Abstract

    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.

    Metadata

    Item Type: Article
    Additional Information: Corrigendum at http://dx.doi.org/10.1016/j.jsb.2016.01.001
    Keyword(s) / Subject(s): Potato cathepsin D inhibitor, Kunitz-type protease inhibitor, Protein X-ray structure, Reactive-site loop, Docking
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Research Centre: Birkbeck Knowledge Lab
    Depositing User: Administrator
    Date Deposited: 03 Nov 2015 17:54
    Last Modified: 02 Dec 2016 13:26
    URI: http://eprints.bbk.ac.uk/id/eprint/13331

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