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Structure of potato cathepsin D inhibitorStructure of potato cathepsin D inhibitor
Structural highlights
FunctionAPI11_SOLTU Inhibitor of cathepsin D (aspartic protease) and trypsin (serine protease). May protect the plant by inhibiting proteases of invading organisms. Publication Abstract from PubMedPotato 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 2.1A showing that PDI adopts a beta-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. Structure of a Kunitz-type potato cathepsin D inhibitor.,Guo J, Erskine PT, Coker AR, Wood SP, Cooper JB J Struct Biol. 2015 Dec;192(3):554-60. doi: 10.1016/j.jsb.2015.10.020. Epub 2015 , Nov 2. PMID:26542926[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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