Structural highlights
Function
API11_SOLTU Inhibitor of cathepsin D (aspartic protease) and trypsin (serine protease). May protect the plant by inhibiting proteases of invading organisms.
Publication Abstract from PubMed
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 2.1A 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
- ↑ Guo J, Erskine PT, Coker AR, Wood SP, Cooper JB. Structure of a Kunitz-type potato cathepsin D inhibitor. J Struct Biol. 2015 Dec;192(3):554-60. doi: 10.1016/j.jsb.2015.10.020. Epub 2015 , Nov 2. PMID:26542926 doi:http://dx.doi.org/10.1016/j.jsb.2015.10.020
