3elo: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
{{STRUCTURE_3elo| PDB=3elo | SCENE= }}
==Crystal Structure of Human Pancreatic Prophospholipase A2==
===Crystal Structure of Human Pancreatic Prophospholipase A2===
<StructureSection load='3elo' size='340' side='right' caption='[[3elo]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
{{ABSTRACT_PUBMED_19297324}}
== 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.


==Function==
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>
[[http://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>


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[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].
</div>


==See Also==
==See Also==
*[[Phospholipase A2|Phospholipase A2]]
*[[Phospholipase A2|Phospholipase A2]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:019297324</ref><references group="xtra"/><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]]
Retrieved from "https://proteopedia.org/3elo"