Sandbox Reserved 919: Difference between revisions
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This is the structure of the enzyme. | This is the structure of the enzyme. | ||
<scene name='57/ | <scene name='57/573134/Generic_monomer/3'>Default Scene in Applet</scene> | ||
<scene name='57/573133/Ligand_showing/1'>Ligand Bound</scene> | <scene name='57/573133/Ligand_showing/1'>Ligand Bound</scene> | ||
</StructureSection> | </StructureSection> | ||
===References=== | |||
{{reflist}} |
Revision as of 21:10, 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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IntroductionIntroduction
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]
StructureThis is the structure of the enzyme.
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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