Sandbox Reserved 919
From Proteopedia
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Revision as of 18:10, 28 March 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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Image:MGLProt.jpg
Monomer of MGL created in PYMOL (PDB:3PE6)
Introduction
Monoglyceride Lipase (MGL, MAGL, MGLL) is a 33 kDa protein found mostly in the cell membrane. It is a member of the serine hydrolase superfamily and is also classified as part of the α/β hydrolase fold family. MGL plays a key role in the hydrolysis of 2-arachidonoylglycerol (2-AG), an endocannabinoid that exists in neurons of the central nervous system, into arachidonic acid and glycerol. 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
