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Monoglyceride LipaseMonoglyceride Lipase

IntroductionIntroduction

File:MGLProt.jpg

Monomer of MGL created in PYMOL (PDB:3PE6)

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]

Structure

Active Site

ReferencesReferences

↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Nathan Alexander Holt, Steven Han, Gregory Zemtsov, R. Jeremy Johnson

[1] 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

[1]

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