View source for 3pe6


==Crystal Structure of a soluble form of human MGLL in complex with an inhibitor==
<StructureSection load='3pe6' size='340' side='right'caption='[[3pe6]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3pe6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PE6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZYH:(2-CYCLOHEXYL-1,3-BENZOXAZOL-6-YL){3-[4-(PYRIMIDIN-2-YL)PIPERAZIN-1-YL]AZETIDIN-1-YL}METHANONE'>ZYH</scene></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=3pe6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pe6 OCA], [https://pdbe.org/3pe6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pe6 RCSB], [https://www.ebi.ac.uk/pdbsum/3pe6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pe6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MGLL_HUMAN MGLL_HUMAN] Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain (By similarity). Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth.<ref>PMID:20079333</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A high-resolution structure of a ligand-bound, soluble form of human monoglyceride lipase is presented. The structure highlights a novel conformation of the regulatory lid-domain present in the lipase family as well as the binding mode of a pharmaceutically relevant reversible inhibitor. Analysis of the structure lacking the inhibitor indicates that the closed conformation can accommodate the native substrate 2 arachidonoyl glycerol. A model is proposed in which monoglyceride lipase undergoes conformational and electrostatic changes during the catalytic cycle ultimately resulting in its dissociation from the membrane upon completion of the cycle. In addition, the study outlines a successful approach to transform membrane associated proteins, which tend to aggregate upon purification, into a monomeric and soluble form.

Crystal structure of a soluble form of human monoglyceride lipase in complex with an inhibitor at 1.35 A resolution.,Schalk-Hihi C, Schubert C, Alexander R, Bayoumy S, Clemente JC, Deckman I, Desjarlais RL, Dzordzorme KC, Flores CM, Grasberger B, Kranz JK, Lewandowski F, Liu L, Ma H, Maguire D, Macielag MJ, McDonnell ME, Haarlander TM, Miller R, Milligan C, Reynolds C, Kuo LC Protein Sci. 2011 Feb 3. doi: 10.1002/pro.596. PMID:21308848<ref>PMID:21308848</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3pe6" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Schalk-Hih C]]
[[Category: Schubert C]]