5dzu: Difference between revisions
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<StructureSection load='5dzu' size='340' side='right'caption='[[5dzu]], [[Resolution|resolution]] 2.12Å' scene=''> | <StructureSection load='5dzu' size='340' side='right'caption='[[5dzu]], [[Resolution|resolution]] 2.12Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5dzu]] is a 2 chain structure with sequence from [ | <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='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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.12Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Solanum tuberosum]] | [[Category: Solanum tuberosum]] | ||
[[Category: Coker | [[Category: Coker AR]] | ||
[[Category: Cooper | [[Category: Cooper JB]] | ||
[[Category: Erskine | [[Category: Erskine P]] | ||
[[Category: Guo | [[Category: Guo J]] | ||
[[Category: Wood | [[Category: Wood SP]] | ||
Latest revision as of 01:08, 29 June 2023
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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