Sandbox Reserved 919: Difference between revisions
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<StructureSection load='3PE6' size='300' frame='true' align='right' caption= 'Structure' scene='57/573133/Generic_monomer/3'> | <StructureSection load='3PE6' size='300' frame='true' align='right' caption= 'Structure' scene='57/573133/Generic_monomer/3'> | ||
===3D Structure=== | ===3D Structure=== | ||
The first complete crystal structure of MGL was determined in 2009 in its apo form. <ref name="bert" /> MGL is a part of the α-β hydrolase family of enzymes.<ref name="labar" /><ref name="bert" /><ref name="shalk" /> This category of proteins contains an <scene name='57/573134/Beta_sheet/ | The first complete crystal structure of MGL was determined in 2009 in its apo form. <ref name="bert" /> MGL is a part of the α-β hydrolase family of enzymes.<ref name="labar" /><ref name="bert" /><ref name="shalk" /> This category of proteins contains an <scene name='57/573134/Beta_sheet/6'>eight-stranded</scene> [http://en.wikipedia.org/wiki/Beta_sheet beta sheet], specifically containing seven parallel and one antiparallel constituent strand, <scene name='57/573134/Beta_sheet/5'>surrounded</scene> by [http://en.wikipedia.org/wiki/Alpha_helix alpha-helices]. <ref name="bert" /> | ||
MGL has a characteristic lid domain comprised of two large loops that surround <scene name='57/573134/Helix_a4/1'>helix A4</scene>.<ref name="bert" /> This region of the enzyme is the membrane-interacting moiety of the protein, which is consistent with its [http://en.wikipedia.org/wiki/Amphiphile amphipathic] nature and outward-facing <scene name='57/573134/Helix_a4/2'>hydrophobic residues</scene> (graphite being nonpolar and cyan being highly polar). 2-AG and other lipids suspended in the hydrophobic section of the cell membrane have been proposed to associate with this region of MGL before entering the active tunnel.<ref name="bert" /> Interestingly, MGL’s lid domain may be more flexible than its analogs in other α-β hydrolases, due to the various conformations it assumed in [http://en.wikipedia.org/wiki/Crystallography crystallographic studies]. <ref name="bert" /> Currently, there is no consensus regarding the quaternary arrangement of MGL. Some studies show that MGL is primarily found as a [http://en.wikipedia.org/wiki/Monomer monomer], <ref name="bert" /> <ref name="shalk" /> whereas other studies have found it to be a physiologically active <scene name='57/573134/Dimer/1'>dimer</scene>. <ref name="labar" /> One compelling piece of evidence for the dimeric quartenary structure is the presence of a <scene name='57/573134/Beta_strand_pair/5'>precisely aligned</scene> pair of beta strands between the two molecules of MGL in [http://www.rcsb.org/pdb/explore.do?structureId=3jw8 3JW8]. | MGL has a characteristic lid domain comprised of two large loops that surround <scene name='57/573134/Helix_a4/1'>helix A4</scene>.<ref name="bert" /> This region of the enzyme is the membrane-interacting moiety of the protein, which is consistent with its [http://en.wikipedia.org/wiki/Amphiphile amphipathic] nature and outward-facing <scene name='57/573134/Helix_a4/2'>hydrophobic residues</scene> (graphite being nonpolar and cyan being highly polar). 2-AG and other lipids suspended in the hydrophobic section of the cell membrane have been proposed to associate with this region of MGL before entering the active tunnel.<ref name="bert" /> Interestingly, MGL’s lid domain may be more flexible than its analogs in other α-β hydrolases, due to the various conformations it assumed in [http://en.wikipedia.org/wiki/Crystallography crystallographic studies]. <ref name="bert" /> Currently, there is no consensus regarding the quaternary arrangement of MGL. Some studies show that MGL is primarily found as a [http://en.wikipedia.org/wiki/Monomer monomer], <ref name="bert" /> <ref name="shalk" /> whereas other studies have found it to be a physiologically active <scene name='57/573134/Dimer/1'>dimer</scene>. <ref name="labar" /> One compelling piece of evidence for the dimeric quartenary structure is the presence of a <scene name='57/573134/Beta_strand_pair/5'>precisely aligned</scene> pair of beta strands between the two molecules of MGL in [http://www.rcsb.org/pdb/explore.do?structureId=3jw8 3JW8]. | ||