Structure of a Kunitz-type potato cathepsin D inhibitor

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 2.1Å showing that PDI adopts a β-trefoil fold, which is typical of the...

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Bibliographic Details
Published in:Journal of structural biology 2015-12, Vol.192 (3), p.554-560
Main Authors: Guo, Jingxu, Erskine, Peter T., Coker, Alun R., Wood, Steve P., Cooper, Jonathan B.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Catalytic Domain - physiology
Cathepsin D - antagonists & inhibitors
Crystallography, X-Ray
Docking
Humans
Kunitz-type protease inhibitor
Models, Molecular
Molecular Docking Simulation
Molecular Sequence Data
Peptides - metabolism
Plant Proteins - metabolism
Plant Proteins - ultrastructure
Potato cathepsin D inhibitor
Protein X-ray structure
Reactive-site loop
Sequence Alignment
Solanum tuberosum - metabolism
Trypsin - metabolism
Trypsin Inhibitors - metabolism
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Summary: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 2.1Å 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.
ISSN:1047-8477
1095-8657
DOI:10.1016/j.jsb.2015.10.020