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Structure of a Kunitz-type potato cathepsin D inhibitor

DOI: 10.1016/j.jsb.2015.10.020 DOI Help
PMID: 26542926 PMID Help

Authors: Jingxu Guo (University College London (UCL)) , Peter Erskine (Royal Free and University College Medical School) , Alun Coker (University College Medical School, UCL Divisision of Medicine) , Steve P. Wood (UCL) , Jonathan Cooper (University College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Structural Biology , VOL 192 (3) , PAGES 554–560

State: Published (Approved)
Published: November 2015
Diamond Proposal Number(s): 8922

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.

Journal Keywords: Potato Cathepsin D Inhibitor; Kunitz-Type Protease Inhibitor; Protein X-Ray Structure; Reactive-Site Loop; Docking

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 08/11/2015 19:29

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