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- W2120769673 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 of this unusual bi-functional inhibitor." @default.
- W2120769673 created "2016-06-24" @default.
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- W2120769673 date "2015-12-01" @default.
- W2120769673 modified "2023-09-26" @default.
- W2120769673 title "Structure of a Kunitz-type potato cathepsin D inhibitor" @default.
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- W2120769673 doi "https://doi.org/10.1016/j.jsb.2015.10.020" @default.
- W2120769673 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26542926" @default.
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