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Monoglyceride Lipase (MGL)

<StructureSection load= size='450' side='right' scene='58/580299/Human_monoglyceride_lipase/1' caption='Bovine aconitase showing FeS4 cluster complex with sulfate (PDB code 1amj)'>

Crystal Structure of MGL

Background

Monoglyceride lipase is part of the α/β hydrolase family, having a Ser-His-Asp catalytic triad (Celemnte et al. 2012). MGL terminates the signaling of a primary endocannabinoid, 2-AG (Savinainen et al 2010). MGL is able to hydrolyze 2-arachidonoylglycerol into arachidonic acid and glycerol (Bertrand et al. 2010). One of the key features of MGL is the hydrophobic tunnel, which has been suggested to provide a model for drug research.

Catalytic triad

Catalytic Triad of MGL structure

Ligand Binding Site

Ligand within the Overall Structure of MGL