Sandbox Reserved 922: Difference between revisions

The <scene name='57/573136/Starting_view/1'>surface</scene> of FAAH reveals two equivalent openings (<scene name='57/573136/Starting_view/4'>Opening 1</scene>, <scene name='57/573136/Starting_view/5'>Opening 2</scene>) directly accessible by the inner layer of the [http://en.wikipedia.org/wiki/Lipid_bilayer lipid bilayer].<ref name= "1MT5">PMID:12459591</ref>  These <scene name='57/573136/Membrane_access_channel/8'>Membrane Access Channels</scene> (MAC) are made up of three flaps and two intrusions which collectively form the entry way for the aliphatic binding of the amide lipid substrate.  Flaps 1 and 2 envelope the middle and backside of the anandamide mimic, and are locked together by a <scene name='57/573136/Membrane_access_channel/9'>salt bridge</scene> between Arg486 and Asp403.  Flap 2 contains a very <scene name='57/573136/Membrane_access_channel/12'>hydrophobic membrane binding cap</scene> that partially covers the opening with Phe432. This binding cap clings to the cell's hydrophobic inner membrane and uses a multitude of <scene name='57/573136/Membrane_access_channel/13'>positively charged residues</scene> to lure out partitioned anandamide by its narrow partial  negative charge. The catalytic site is defined by the catalytic triad:  the <scene name='57/573136/Membrane_access_channel/14'>238-241 anionic hole loop</scene> contributes the nucleophilic S241, loop 3 contributes the neighboring <scene name='57/573136/Membrane_access_channel/15'>S217</scene> upon forming the very top of the membrane access channel, and a fourth loop contributes the K142.  

The membrane access channel leads to the active site, which is flanked by  both the <scene name='57/573136/Cytosolic_port/2'>acyl chain binding pocket and cytosolic port </scene> (ABP and CP).<ref name= "3LJ7">PMID:20493882</ref> The cytosolic port is a lengthy, flexible loop that leads directly into the [http://en.wikipedia.org/wiki/Cytoplasm cytoplasm], allowing the deacylated amine to enter the cell.

</StructureSection >the