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3elo
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3elo.png|left|200px]] | ||
| - | < | + | ==Crystal Structure of Human Pancreatic Prophospholipase A2== |
| - | + | <StructureSection load='3elo' size='340' side='right'caption='[[3elo]], [[Resolution|resolution]] 1.55Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3elo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ELO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ELO FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | -- | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLA2G1B ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [https://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=3elo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3elo OCA], [https://pdbe.org/3elo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3elo RCSB], [https://www.ebi.ac.uk/pdbsum/3elo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3elo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/PA21B_HUMAN PA21B_HUMAN]] PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides, this releases glycerophospholipids and arachidonic acid that serve as the precursors of signal molecules.<ref>PMID:19297324</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/el/3elo_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3elo ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pancreatic phospholipase A2 (phospholipase A2 group 1B, G1B) belongs to the superfamily of secreted phospholipase A2 (PLA2) enzymes. G1B has been proposed to be a potential target for diseases such as hypertension, obesity, and diabetes. Human pancreatic prophospholipase A2 (pro-hG1B) is activated by cleavage of the first seven-residue propeptide (phospholipase A2 propeptide, PROP). However, questions still remain on the mode of action for pro-hG1B. In this work, we expressed pro-hG1B in Pichia pastoris and determined the crystal structure at 1.55-A resolution. The x-ray structure demonstrates that pro-hG1B forms a trimer. In addition, PROP occupies the catalytic cavity and can be self-cleaved at 37 degrees C. A new membrane-bound surface and activation mechanism are proposed based on the trimeric model of pro-hG1B. We also propose a new autoproteolytic mechanism for pro-hG1B by the reaction triad Asp49-Arg0-Ser(-2) that is similar to the serine protease catalytic triad. | ||
| - | + | Structural insight into the activation mechanism of human pancreatic prophospholipase A2.,Xu W, Yi L, Feng Y, Chen L, Liu J J Biol Chem. 2009 Jun 12;284(24):16659-66. Epub 2009 Mar 18. PMID:19297324<ref>PMID:19297324</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3elo" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Human]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Chen, L]] | |
| - | == | + | [[Category: Feng, Y]] |
| - | < | + | [[Category: Liu, J]] |
| - | [[Category: | + | [[Category: Xu, W]] |
| - | [[Category: Chen, L | + | [[Category: Yi, L]] |
| - | [[Category: Feng, Y | + | |
| - | [[Category: Liu, J | + | |
| - | [[Category: Xu, W | + | |
| - | [[Category: Yi, L | + | |
| - | + | ||
[[Category: Human pancreatic prophospholipase a2]] | [[Category: Human pancreatic prophospholipase a2]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Lipid degradation]] | [[Category: Lipid degradation]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
| - | [[Category: Polymorphism]] | ||
[[Category: Secreted]] | [[Category: Secreted]] | ||
[[Category: Trimeric]] | [[Category: Trimeric]] | ||
| - | |||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 22 10:41:50 2009'' | ||
Current revision
Crystal Structure of Human Pancreatic Prophospholipase A2
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Categories: Human | Large Structures | Chen, L | Feng, Y | Liu, J | Xu, W | Yi, L | Human pancreatic prophospholipase a2 | Hydrolase | Lipid degradation | Metal-binding | Secreted | Trimeric

