3elo
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal Structure of Human Pancreatic Prophospholipase A2== | |
- | === | + | <StructureSection load='3elo' size='340' side='right' caption='[[3elo]], [[Resolution|resolution]] 1.55Å' scene=''> |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[3elo]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ELO FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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 ([http://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'>[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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3elo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3elo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3elo RCSB], [http://www.ebi.ac.uk/pdbsum/3elo PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == 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/chain_selection.php?pdb_ID=2ata 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> | |
==See Also== | ==See Also== | ||
*[[Phospholipase A2|Phospholipase A2]] | *[[Phospholipase A2|Phospholipase A2]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
- | [[Category: Chen, L | + | [[Category: Chen, L]] |
- | [[Category: Feng, Y | + | [[Category: Feng, Y]] |
- | [[Category: Liu, J | + | [[Category: Liu, J]] |
- | [[Category: Xu, W | + | [[Category: Xu, W]] |
- | [[Category: Yi, L | + | [[Category: Yi, L]] |
[[Category: Human pancreatic prophospholipase a2]] | [[Category: Human pancreatic prophospholipase a2]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] |
Revision as of 18:07, 21 December 2014
Crystal Structure of Human Pancreatic Prophospholipase A2
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Categories: Human | Chen, L | Feng, Y | Liu, J | Xu, W | Yi, L | Human pancreatic prophospholipase a2 | Hydrolase | Lipid degradation | Metal-binding | Secreted | Trimeric