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| | <StructureSection load='3qlm' size='340' side='right'caption='[[3qlm]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='3qlm' size='340' side='right'caption='[[3qlm]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qlm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QLM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QLM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qlm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QLM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o4m|3o4m]], [[3hsw|3hsw]], [[3l30|3l30]], [[3l69|3l69]], [[2b00|2b00]], [[2b01|2b01]], [[2b04|2b04]], [[2b03|2b03]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span></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=3qlm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qlm OCA], [https://pdbe.org/3qlm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qlm RCSB], [https://www.ebi.ac.uk/pdbsum/3qlm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qlm ProSAT]</span></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=3qlm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qlm OCA], [http://pdbe.org/3qlm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qlm RCSB], [http://www.ebi.ac.uk/pdbsum/3qlm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qlm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PA21B_PIG PA21B_PIG]] PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | + | [https://www.uniprot.org/uniprot/PA21B_PIG PA21B_PIG] PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Phospholipase A2|Phospholipase A2]] | + | *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Sus scrofa]] | | [[Category: Sus scrofa]] |
| - | [[Category: Aparna, V]] | + | [[Category: Aparna V]] |
| - | [[Category: Dileep, K V]] | + | [[Category: Dileep KV]] |
| - | [[Category: Haridas, M]] | + | [[Category: Haridas M]] |
| - | [[Category: Karthe, P]] | + | [[Category: Karthe P]] |
| - | [[Category: Mandal, P K]] | + | [[Category: Mandal PK]] |
| - | [[Category: Sadasivan, C]] | + | [[Category: Sadasivan C]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Palmitic acid binding]]
| + | |
| - | [[Category: Pancreatic enzyme]]
| + | |
| - | [[Category: Pla2]]
| + | |
| Structural highlights
Function
PA21B_PIG PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Publication Abstract from PubMed
Ester bond hydrolysis of membrane phospholipids by Phospholipase A(2) and consequent release of fatty acids is the initiating step of inflammation. It is proposed here that the inhibition of PLA(2) is one of the ways to control inflammation. Investigations are done to identify the mode of inhibition of PLA(2) by the n-hexadecanoic acid. It may help designing of specific inhibitors of PLA(2) as anti-inflammatory agents. The enzyme kinetics study proved that n-hexadecanoic acid inhibits PLA(2) in a competitive manner. It was identified from the crystal structure at 2.5A resolution that the position of n-hexadecanoic acid is in the active site of the PLA(2) . The binding constant and binding energy have also been calculated using Isothermal Titration Calorimetry. Also, the binding energy of n-hexadecanoic acid to PLA(2) was calculated by in silico method and compared with known inhibitors. It may be concluded from the structural and kinetics studies that the fatty acid, n-hexadecanoic acid, is an inhibitor of PLA(2) . The inferences from the present study validate the rigorous use of medicated oils rich in n-hexadecanoic acid for the treatment of rheumatic symptoms in the traditional medical system of India, Ayurveda. (c) 2012 John Wiley & Sons A/S.
Anti-inflammatory property of n-hexadecanoic acid: Structural evidence and Kinetic assessment.,Aparna V, Dileep KV, Mandal PK, Karthe P, Sadasivan C, Haridas M Chem Biol Drug Des. 2012 May 29. doi: 10.1111/j.1747-0285.2012.01418.x. PMID:22642495[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Aparna V, Dileep KV, Mandal PK, Karthe P, Sadasivan C, Haridas M. Anti-inflammatory property of n-hexadecanoic acid: Structural evidence and Kinetic assessment. Chem Biol Drug Des. 2012 May 29. doi: 10.1111/j.1747-0285.2012.01418.x. PMID:22642495 doi:10.1111/j.1747-0285.2012.01418.x
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