Sandbox Reserved 919
From Proteopedia
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==Introduction== | ==Introduction== | ||
[[Image:MGLProt.jpg|300 px|right|thumb|Monomer of MGL created in PYMOL (PDB:3PE6)]] | [[Image:MGLProt.jpg|300 px|right|thumb|Monomer of MGL created in PYMOL (PDB:3PE6)]] | ||
| - | '''Monoglyceride Lipase''' ('''MGL''', '''MAGL''', '''MGLL''') is a 33 kDa [http://en.wikipedia.org/wiki/Protein protein] found mostly in the cell membrane. It is a [http://en.wikipedia.org/wiki/Serine_hydrolase serine hydrolase] enzyme that exhibits an [http://en.wikipedia.org/wiki/Alpha/beta_hydrolase_fold α/β hydrolase fold]. MGL plays a key role in the hydrolysis of 2-arachidonoylglycerol (2-AG), an endocannabinoid produced by the the central nervous system | + | '''Monoglyceride Lipase''' ('''MGL''', '''MAGL''', '''MGLL''') is a 33 kDa [http://en.wikipedia.org/wiki/Protein protein] found mostly in the cell membrane. It is a [http://en.wikipedia.org/wiki/Serine_hydrolase serine hydrolase] enzyme that exhibits an [http://en.wikipedia.org/wiki/Alpha/beta_hydrolase_fold α/β hydrolase fold]. In addition, MGL possesses amphitropic character, where the area around the active site of MGL is polar while the site itself is non-polar. This characteristic allows the protein to be present both in the membrane and in the cytosol. MGL plays a key role in the hydrolysis of 2-arachidonoylglycerol (2-AG), an endocannabinoid produced by the the central nervous system. The α/β fold allows 2-AG to selectively bind to the active site and be broken down into arachidonic acid and glycerol. Upon breakdown, glycerol leaves via an "exit tunnel" found perpendicular to the α/β fold. 2-AG itself has been found to possess anti-nociceptive, immunomodulatory, anti-inflammatory and tumor-reductive character when it binds to cannabinoid receptors. Due to the vast medical and therapeutic utility of 2-AG, the inhibition of MGL is a high interest target in pharmaceutical research. <ref> PMID:19962385 </ref> |
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<scene name='57/573133/Ligand_showing/1'>Ligand Bound</scene> | <scene name='57/573133/Ligand_showing/1'>Ligand Bound</scene> | ||
<p><scene name='57/573134/Catalytic_triad/2'>Catalytic Triad</scene></p> | <p><scene name='57/573134/Catalytic_triad/2'>Catalytic Triad</scene></p> | ||
| + | <p><scene name='57/573134/Oxyanion_hole/1'>Oxyanion Hole</scene></p> | ||
</StructureSection> | </StructureSection> | ||
Revision as of 03:59, 3 April 2014
| This Sandbox is Reserved from Jan 06, 2014, through Aug 22, 2014 for use by the Biochemistry II class at the Butler University at Indianapolis, IN USA taught by R. Jeremy Johnson. This reservation includes Sandbox Reserved 911 through Sandbox Reserved 922. |
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Monoglyceride Lipase
Introduction
Monoglyceride Lipase (MGL, MAGL, MGLL) is a 33 kDa protein found mostly in the cell membrane. It is a serine hydrolase enzyme that exhibits an α/β hydrolase fold. In addition, MGL possesses amphitropic character, where the area around the active site of MGL is polar while the site itself is non-polar. This characteristic allows the protein to be present both in the membrane and in the cytosol. MGL plays a key role in the hydrolysis of 2-arachidonoylglycerol (2-AG), an endocannabinoid produced by the the central nervous system. The α/β fold allows 2-AG to selectively bind to the active site and be broken down into arachidonic acid and glycerol. Upon breakdown, glycerol leaves via an "exit tunnel" found perpendicular to the α/β fold. 2-AG itself has been found to possess anti-nociceptive, immunomodulatory, anti-inflammatory and tumor-reductive character when it binds to cannabinoid receptors. Due to the vast medical and therapeutic utility of 2-AG, the inhibition of MGL is a high interest target in pharmaceutical research. [1]
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References
- ↑ Bertrand T, Auge F, Houtmann J, Rak A, Vallee F, Mikol V, Berne PF, Michot N, Cheuret D, Hoornaert C, Mathieu M. Structural basis for human monoglyceride lipase inhibition. J Mol Biol. 2010 Feb 26;396(3):663-73. Epub 2009 Dec 3. PMID:19962385 doi:10.1016/j.jmb.2009.11.060
