Sandbox Reserved 921: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, R. Jeremy Johnson, Carter Sharp, Daniel B. Lange

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 <StructureSection load='4J5P' size='340' side='right' caption='4HBP; K and L of 1MT5' scene='57/573135/Ser241_4j5p/1'>
+== Function ==
+The fatty acid amide hydrolase cleaves fatty acid amides at the carbon-oxygen double bond in the amide functional group.  The lipid-degrading activity of FAAH derives from its unusual <scene name='57/573135/Catalytic_triad/2'>catalytic triad</scene>, consisting of Ser241, Ser217, and Lys142.  The hydrogen bonding between the three amino acid residues allows for a partial negative charge at Ser241, which acts as a nucleophile in the enzymatic reaction.  The Ser241 residue binds with the carbon in the amide group, cleaves the fatty acid amide, and is protonated by water.  The inhibitor used covalently binds to Ser241 disrupting the catalytic triad active site and leaving the hydrolase inactive.  Without the enzyme FAAH active, anandamide levels increase causing pain relief due to anandamide interacting with the CB1 and CB2 cannabinoid receptors.
 <scene name='57/573135/Ser241_4j5p/1'>Ser241 bound to ligand</scene>
 <scene name='57/573135/4j5p_dimer/3'>Dimer</scene>
-<scene name='57/573135/Catalytic_triad/2'>Catalytic Triad</scene>
 This is the overall <scene name='57/573136/Starting_view/1'>Dimer</scene>.  The membrane access channel is accessible to lipids partitioned in the inner layer of the lipid bilayer.  This is the <scene name='57/573136/Membrane_access_channel/4'>Membrane Access Channel (MAC)</scene>.  This is the <scene name='57/573136/Cytosolic_port/2'>Acyl Chain Binding Pocket (ABP) and Cytosolic Port (CP)</scene>.