View source for 5dzu


==Structure of potato cathepsin D inhibitor==
<StructureSection load='5dzu' size='340' side='right'caption='[[5dzu]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dzu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DZU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.12&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dzu OCA], [https://pdbe.org/5dzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dzu RCSB], [https://www.ebi.ac.uk/pdbsum/5dzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dzu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/API11_SOLTU API11_SOLTU] Inhibitor of cathepsin D (aspartic protease) and trypsin (serine protease). May protect the plant by inhibiting proteases of invading organisms.
<div style="background-color:#fffaf0;">
== 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<ref>PMID:26542926</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5dzu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Solanum tuberosum]]
[[Category: Coker AR]]
[[Category: Cooper JB]]
[[Category: Erskine P]]
[[Category: Guo J]]
[[Category: Wood SP]]