5dzu: Difference between revisions
No edit summary |
No edit summary |
||
| Line 8: | Line 8: | ||
== Function == | == Function == | ||
[[http://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. | [[http://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®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 00:23, 1 December 2015
Structure of potato cathepsin D inhibitorStructure of potato cathepsin D inhibitor
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 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
|
| ||||||||||||||||