Sandbox Reserved 922: Difference between revisions

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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 the which collectively allow the entry and 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 hydrophobic membrane binding cap.  This binding cap clings to the cell's inner membrane and lures out partitioned anandamide by attracting the substrate's narrow partially negatively charged head group with a multitude of positively charged residues.  its  each proceed by a respective membrane binding cap.  This sturdy flap appears to be loosened by the presence of five positively charged residues, and each MAC remains conformation-stable by a salt bridge.  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.
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.  


</StructureSection >
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

Latest revision as of 19:24, 25 April 2014

This Sandbox is Reserved from Jan 06, 2014, through Aug 22, 2014 for use by the Biochemistry II class at the Butler University at Indianapolis, IN USA taught by R. Jeremy Johnson. This reservation includes Sandbox Reserved 911 through Sandbox Reserved 922.
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This is the overall . The membrane access channel is accessible to lipids partitioned in the inner layer of the lipid bilayer. This is the . This is the .


The of FAAH reveals two equivalent openings (, ) directly accessible by the inner layer of the lipid bilayer.[1] These (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 between Arg486 and Asp403. Flap 2 contains a very that partially covers the opening with Phe432. This binding cap clings to the cell's hydrophobic inner membrane and uses a multitude of to lure out partitioned anandamide by its narrow partial negative charge. The catalytic site is defined by the catalytic triad: the contributes the nucleophilic S241, loop 3 contributes the neighboring 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 (ABP and CP).[2] The cytosolic port is a lengthy, flexible loop that leads directly into the cytoplasm, allowing the deacylated amine to enter the cell.


Chains K and L from 1MT5

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the

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OCA, Daniel B. Lange
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