3s8j: Difference between revisions
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==Crystal structure of a papaya latex serine protease inhibitor (PPI) at 2.6A resolution== | |||
<StructureSection load='3s8j' size='340' side='right' caption='[[3s8j]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3s8j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Carica_papaya Carica papaya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S8J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S8J FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3s8k|3s8k]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3s8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s8j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s8j RCSB], [http://www.ebi.ac.uk/pdbsum/3s8j PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Proteases carry out a number of crucial functions inside and outside the cell. To protect the cells against the potentially lethal activities of these enzymes, specific inhibitors are produced to tightly regulate the protease activity. Independent reports suggest that the Kunitz-soybean trypsin inhibitor (STI) family has the potential to inhibit proteases with different specificities. In this study, we use a combination of biophysical methods to define the structural basis of the interaction of papaya protease inhibitor (PPI) with serine proteases. We show that PPI is a multiple-headed inhibitor; a single PPI molecule can bind two trypsin units at the same time. Based on sequence and structural analysis, we hypothesize that the inherent plasticity of the beta-trefoil fold is paramount in the functional evolution of this family toward multiple protease inhibition. | |||
The plasticity of the beta-trefoil fold constitutes an evolutionary platform for protease inhibition.,Azarkan M, Martinez-Rodriguez S, Buts L, Baeyens-Volant D, Garcia-Pino A J Biol Chem. 2011 Dec 23;286(51):43726-34. Epub 2011 Oct 25. PMID:22027836<ref>PMID:22027836</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Carica papaya]] | [[Category: Carica papaya]] | ||
[[Category: Garcia-Pino, A | [[Category: Garcia-Pino, A]] | ||
[[Category: Hydrolase inhibitor]] | [[Category: Hydrolase inhibitor]] | ||
[[Category: Kunitz-sti fold]] | [[Category: Kunitz-sti fold]] | ||
[[Category: Serine protease inhibitor]] | [[Category: Serine protease inhibitor]] | ||
Revision as of 09:36, 21 December 2014
Crystal structure of a papaya latex serine protease inhibitor (PPI) at 2.6A resolutionCrystal structure of a papaya latex serine protease inhibitor (PPI) at 2.6A resolution
Structural highlights
Publication Abstract from PubMedProteases carry out a number of crucial functions inside and outside the cell. To protect the cells against the potentially lethal activities of these enzymes, specific inhibitors are produced to tightly regulate the protease activity. Independent reports suggest that the Kunitz-soybean trypsin inhibitor (STI) family has the potential to inhibit proteases with different specificities. In this study, we use a combination of biophysical methods to define the structural basis of the interaction of papaya protease inhibitor (PPI) with serine proteases. We show that PPI is a multiple-headed inhibitor; a single PPI molecule can bind two trypsin units at the same time. Based on sequence and structural analysis, we hypothesize that the inherent plasticity of the beta-trefoil fold is paramount in the functional evolution of this family toward multiple protease inhibition. The plasticity of the beta-trefoil fold constitutes an evolutionary platform for protease inhibition.,Azarkan M, Martinez-Rodriguez S, Buts L, Baeyens-Volant D, Garcia-Pino A J Biol Chem. 2011 Dec 23;286(51):43726-34. Epub 2011 Oct 25. PMID:22027836[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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