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Dominique Stephens, Erica Yothment

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 [[Image:Complete_crystal_structure.png|left|300px|thumb|'''Figure 1:'''Crystal Structure of MGL Alpha helixes are in blue and beta sheets in purple. This protein is a dimer that is linked by antiparallel beta sheets]]
 ==Background==
-Monoglyceride [[:Category:Lipase| Lipase]] (MGL) is part of the α/β hydrolase family,a [[:Category:Serine hydrolase| Serine hydrolase]] (Figure 1), having a <scene name='58/580298/Catalytic_triad/4'>Ser-His-Asp catalytic triad </scene> <ref name="Clemente">[Clemente, J. C., E. Nulton, M. Nelen, M. J. Todd, D. Maguire, C. Schalk-Hihi, L. C. Kuo, S.-P. Zhang, C. M. Flores, and J. K. Kranz. "Screening and Characterization of Human Monoglyceride Lipase Active Site Inhibitors Using Orthogonal Binding and Functional Assays." Journal of Biomolecular Screening 17.5 (2012): 629-40]</ref>. [http://en.wikipedia.org/wiki/Monoacylglycerol_lipase MGL] is present in most cells, providing the rate limiting step for  the hydrolysis of [http://en.wikipedia.org/wiki/Monoglyceride monoacylglycerols] (MG) into fatty acids and glycerol <ref name="Taschler">[Taschler, U., F. P. W. Radner, C. Heier, R. Schreiber, M. Schweiger, G. Schoiswohl, K. Preiss-Landl, D. Jaeger, B. Reiter, H. C. Koefeler, J. Wojciechowski, C. Theussl, J. M. Penninger, A. Lass, G. Haemmerle, R. Zechner, and R. Zimmermann. "Monoglyceride Lipase Deficiency in Mice Impairs Lipolysis and Attenuates Diet-induced Insulin Resistance." Journal of Biological Chemistry 286.20 (2011): 17467-7477]</ref> .  MGL also terminates the signaling of a primary endocannabinoid, 2-arachidonoyl glycerol (2-AG) <ref name="Savinainen">[Savinainen, Juha R., Megumi Yoshino, Anna Minkkilä, Tapio Nevalainen, and Jarmo T. Laitinen. "Characterization of Binding Properties of Monoglyceride Lipase Inhibitors by a Versatile Fluorescence-based Technique." Analytical Biochemistry 399.1 (2010): 132-34]</ref>. MGL is the main enzyme responsible for hydrolyzing 2-arachidonoylglycerol into arachidonic acid and glycerol ''in vivo'' (Figure 3) <ref name="Bertrand">[ Bertrand, T., F. Augé, J. Houtmann, A. Rak, F. Vallée, V. Mikol, P.f. Berne, N. Michot, D. Cheuret, C. Hoornaert, and M. Mathieu. "Structural Basis for Human Monoglyceride Lipase Inhibition." Journal of Molecular Biology 396.3 (2010): 663-73.]</ref>. One of the key features of MGL is the hydrophobic tunnel, which has been suggested to provide a model for drug research (Figure 7).
+Monoglyceride [[:Category:Lipase| Lipase]] (MGL) is part of the α/β hydrolase family,a [[:Category:Serine hydrolase| Serine hydrolase]] (Figure 1), having a <scene name='58/580298/Catalytic_triad/4'>Ser-His-Asp catalytic triad </scene> <ref name="Clemente">[Clemente, J. C., E. Nulton, M. Nelen, M. J. Todd, D. Maguire, C. Schalk-Hihi, L. C. Kuo, S.-P. Zhang, C. M. Flores, and J. K. Kranz. "Screening and Characterization of Human Monoglyceride Lipase Active Site Inhibitors Using Orthogonal Binding and Functional Assays." Journal of Biomolecular Screening 17.5 (2012): 629-40]</ref>. [http://en.wikipedia.org/wiki/Monoacylglycerol_lipase MGL] is present in most cells, providing the rate limiting step for  the hydrolysis of [http://en.wikipedia.org/wiki/Monoglyceride monoacylglycerols] (MG) into fatty acids and glycerol <ref name="Taschler">[Taschler, U., F. P. W. Radner, C. Heier, R. Schreiber, M. Schweiger, G. Schoiswohl, K. Preiss-Landl, D. Jaeger, B. Reiter, H. C. Koefeler, J. Wojciechowski, C. Theussl, J. M. Penninger, A. Lass, G. Haemmerle, R. Zechner, and R. Zimmermann. "Monoglyceride Lipase Deficiency in Mice Impairs Lipolysis and Attenuates Diet-induced Insulin Resistance." Journal of Biological Chemistry 286.20 (2011): 17467-7477]</ref> .  MGL also terminates the signaling of a primary endocannabinoid, 2-arachidonoyl glycerol (2-AG) <ref name="Savinainen">[Savinainen, Juha R., Megumi Yoshino, Anna Minkkilä, Tapio Nevalainen, and Jarmo T. Laitinen. "Characterization of Binding Properties of Monoglyceride Lipase Inhibitors by a Versatile Fluorescence-based Technique." Analytical Biochemistry 399.1 (2010): 132-34]</ref>. MGL is the main enzyme responsible for hydrolyzing 2-arachidonoylglycerol into arachidonic acid and glycerol ''in vivo'' (Figure 3) <ref name="Bertrand">[ Bertrand, T., F. Augé, J. Houtmann, A. Rak, F. Vallée, V. Mikol, P.f. Berne, N. Michot, D. Cheuret, C. Hoornaert, and M. Mathieu. "Structural Basis for Human Monoglyceride Lipase Inhibition." Journal of Molecular Biology 396.3 (2010): 663-73.]</ref>. One of the key features of MGL is the hydrophobic tunnel, which has been suggested to provide a model for drug research (Figure 7). <ref name="Bertrand" />
 ===Metabolic Role===
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 ==Structure==
-The <scene name='58/580298/Overall_structure/3'>overall structure</scene> of MGL has eight-stranded β-sheet protein fold with seven parallel and one <scene name='58/580299/Beta_sheets/1'> antiparallel strand </scene>. Similar to the other α/β hydrolases, the β-sheets in the center of the protein surrounded by α-helices.  The combination of the α-helices and β-sheets are able to provide a stable scaffold for the active site within MGL. Within the main domain of MGL is the conserved catalytic triad <ref name="Bertrand" />.
+The <scene name='58/580298/Overall_structure/3'>overall structure</scene> of MGL has an eight-stranded β-sheet protein fold with seven parallel and one <scene name='58/580299/Beta_sheets/1'> antiparallel strand </scene>. Similar to the other α/β hydrolases, the β-sheets in the center of the protein surrounded by α-helices.  The combination of the α-helices and β-sheets are able to provide a stable scaffold for the active site within MGL. Within the main domain of MGL is the conserved catalytic triad <ref name="Bertrand" />.
 == Catalytic triad ==