Proteopedia - User contributions [en]

https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Daniel+B.+Lange Proteopedia - User contributions [en] 2026-09-27T07:19:05Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1918306 Sandbox Reserved 921 2014-04-25T16:54:09Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Figure 1: Ser, Ser, Lys Catalytic Triad in FAAH. [http://www.sciencemag.org/content/298/5599/1793 1MT5]]]<br /> <br /> <br /> == Introduction ==<br /> [http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase Fatty acid amide hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of [http://en.wikipedia.org/wiki/Fatty_acid_amide fatty acid amides]. FAAH primarily degrades [http://en.wikipedia.org/wiki/Anandamide anandamide], which is an endocannabinoid that activates the CB1 and CB2 [http://en.wikipedia.org/wiki/Cannabinoid_receptor cannabinoid receptors]. When CB1 and CB2 cannabinoid receptors are active, the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication.<br /> <br /> An inhibitor binds to the active site of the enzyme lowering the rate at which the enzyme degrades substrate, thus enzyme inhibitors are often used as drugs. A FAAH inhibitor offers great potential as a pain relief drug because FAAH commonly degrades anandamide. If the enzymatic activity of FAAH was lowered there would be increased levels of anandamide causing increased appetite, sleep, and pain relief.<br /> <br /> A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site.<ref name="Most Recent Study">PMID:23581831</ref> A humanized rat variant of FAAH was inhibited by BR1, CL, and PEG. The mice displayed an increase in endogenous brain levels of the FAAH substrate anandamide for over six hours.<ref name="Most Recent Study">PMID:23581831</ref> This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4J5P; K and L of 1MT5' scene='57/573135/4j5p_dimer/3'><br /> <br /> == Function ==<br /> The fatty acid amide hydrolase <scene name='57/573135/4j5p_dimer/3'>dimer</scene> is an integral membrane protein that cleaves fatty acid amides at the carbon-oxygen double bond in the amide functional group.<ref name="Wiki FAAH">http://en.wikipedia.org/wiki/FAAH</ref> <br /> <br /> [[Image:Anandamide.png|150 px|left|thumb|Figure 2: Anadamide, hydrolysis substrate of FAAH]]<br /> <br /> 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 <scene name='57/573135/Ser241_4j5p/1'>Ser241</scene>, 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 BR1 covalently binds to Ser241 disrupting the [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] active site and inactivating the [http://en.wikipedia.org/wiki/Hydrolase hydrolase].<ref name= "4HBP">PMID:23218778</ref> Without the active FAAH, anandamide accumulates, resulting in pain relief due to its increased concentration and interaction with the CB1 and CB2 cannabinoid receptors.<br /> <br /> ==Structure==<br /> 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 deprotonating <scene name='57/573136/Membrane_access_channel/16'>K142</scene>. The membrane access channel leads to the active site, which is flanked by both the <scene name='57/573136/Membrane_access_channel/16'>cytosolic port</scene> and the acyl chain binding pocket. 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, while the acyl chain binding pocket is a space formed by several of the loops that accommodates the substrates polar head.<br /> <br /> <br /> <br /> </StructureSection><br /> <br /> <br /> <br /> <br /> == References ==<br /> <br /> <references/></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1918304 Sandbox Reserved 921 2014-04-25T16:43:56Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Figure 1: Ser, Ser, Lys Catalytic Triad in FAAH. [http://www.sciencemag.org/content/298/5599/1793 1MT5]]]<br /> <br /> <br /> == Introduction ==<br /> [http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase Fatty acid amide hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of [http://en.wikipedia.org/wiki/Fatty_acid_amide fatty acid amides]. FAAH primarily degrades [http://en.wikipedia.org/wiki/Anandamide anandamide], which is an endocannabinoid that activates the CB1 and CB2 [http://en.wikipedia.org/wiki/Cannabinoid_receptor cannabinoid receptors]. When CB1 and CB2 cannabinoid receptors are active, the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication.<br /> <br /> An inhibitor binds to the active site of the enzyme lowering the rate at which the enzyme degrades substrate, thus enzyme inhibitors are often used as drugs. A FAAH inhibitor offers great potential as a pain relief drug because FAAH commonly degrades anandamide. If the enzymatic activity of FAAH was lowered there would be increased levels of anandamide causing increased appetite, sleep, and pain relief.<br /> <br /> A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site.<ref name="Most Recent Study">PMID:23581831</ref> A humanized rat variant of FAAH was inhibited by BR1, CL, and PEG. The mice displayed an increase in endogenous brain levels of the FAAH substrate anandamide for over six hours.<ref name="Most Recent Study">PMID:23581831</ref> This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4J5P; K and L of 1MT5' scene='57/573135/4j5p_dimer/3'><br /> <br /> == Function ==<br /> The fatty acid amide hydrolase <scene name='57/573135/4j5p_dimer/3'>dimer</scene> is an integral membrane protein that cleaves fatty acid amides at the carbon-oxygen double bond in the amide functional group.<ref name="Wiki FAAH">http://en.wikipedia.org/wiki/FAAH</ref> <br /> <br /> [[Image:Anandamide.png|150 px|left|thumb|Figure 2: Anadamide, hydrolysis substrate of FAAH]]<br /> <br /> 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 <scene name='57/573135/Ser241_4j5p/1'>Ser241</scene>, 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 BR1 covalently binds to Ser241 disrupting the [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] active site and inactivating the [http://en.wikipedia.org/wiki/Hydrolase hydrolase].<ref name= "4HBP">PMID:23218778</ref> Without the active FAAH, anandamide accumulates, resulting in pain relief due to its increased concentration and interaction with the CB1 and CB2 cannabinoid receptors.<br /> <br /> ==Structure==<br /> 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 deprotonating <scene name='57/573136/Membrane_access_channel/16'>K142</scene>. <br /> <br /> 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.<br /> <br /> <br /> <br /> </StructureSection><br /> <br /> <br /> <br /> <br /> == References ==<br /> <br /> <references/></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1918301 Sandbox Reserved 921 2014-04-25T16:24:59Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Figure 1: Ser, Ser, Lys Catalytic Triad in FAAH. [http://www.sciencemag.org/content/298/5599/1793 1MT5]]]<br /> <br /> <br /> == Introduction ==<br /> [http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase Fatty acid amide hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of [http://en.wikipedia.org/wiki/Fatty_acid_amide fatty acid amides]. FAAH primarily degrades [http://en.wikipedia.org/wiki/Anandamide anandamide], which is an endocannabinoid that activates the CB1 and CB2 [http://en.wikipedia.org/wiki/Cannabinoid_receptor cannabinoid receptors]. When CB1 and CB2 cannabinoid receptors are active, the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication.<br /> <br /> An inhibitor binds to the active site of the enzyme lowering the rate at which the enzyme degrades substrate, thus enzyme inhibitors are often used as drugs. A FAAH inhibitor offers great potential as a pain relief drug because FAAH commonly degrades anandamide. If the enzymatic activity of FAAH was lowered there would be increased levels of anandamide causing increased appetite, sleep, and pain relief.<br /> <br /> A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site.<ref name="Most Recent Study">PMID:23581831</ref> A humanized rat variant of FAAH was inhibited by BR1, CL, and PEG. The mice displayed an increase in endogenous brain levels of the FAAH substrate anandamide for over six hours.<ref name="Most Recent Study">PMID:23581831</ref> This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4J5P; K and L of 1MT5' scene='57/573135/4j5p_dimer/3'><br /> <br /> == Function ==<br /> The fatty acid amide hydrolase <scene name='57/573135/4j5p_dimer/3'>dimer</scene> is an integral membrane protein that cleaves fatty acid amides at the carbon-oxygen double bond in the amide functional group.<ref name="Wiki FAAH">http://en.wikipedia.org/wiki/FAAH</ref> <br /> <br /> [[Image:Anandamide.png|150 px|left|thumb|Figure 2: Anadamide, hydrolysis substrate of FAAH]]<br /> <br /> 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 <scene name='57/573135/Ser241_4j5p/1'>Ser241</scene>, 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 BR1 covalently binds to Ser241 disrupting the [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] active site and inactivating the [http://en.wikipedia.org/wiki/Hydrolase hydrolase].<ref name= "4HBP">PMID:23218778</ref> Without the active FAAH, anandamide accumulates, resulting in pain relief due to its increased concentration and interaction with the CB1 and CB2 cannabinoid receptors.<br /> <br /> ==Structure==<br /> 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. <br /> <br /> 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.<br /> <br /> <br /> <br /> </StructureSection><br /> <br /> <br /> <br /> <br /> == References ==<br /> <br /> <references/></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1918300 Sandbox Reserved 922 2014-04-25T16:24:13Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> 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. <br /> <br /> 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.<br /> <br /> </StructureSection >the</div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1918298 Sandbox Reserved 922 2014-04-25T13:05:05Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> 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 S217 upon forming the very top of the membrane access channel, and a fourth loop contributes the K142. <br /> <br /> 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.<br /> <br /> </StructureSection >the</div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1918297 Sandbox Reserved 921 2014-04-25T11:51:11Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Figure 1: Ser, Ser, Lys Catalytic Triad in FAAH. [http://www.sciencemag.org/content/298/5599/1793 1MT5]]]<br /> <br /> <br /> == Introduction ==<br /> [http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase Fatty acid amide hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of [http://en.wikipedia.org/wiki/Fatty_acid_amide fatty acid amides]. FAAH primarily degrades [http://en.wikipedia.org/wiki/Anandamide anandamide], which is an endocannabinoid that activates the CB1 and CB2 [http://en.wikipedia.org/wiki/Cannabinoid_receptor cannabinoid receptors]. When CB1 and CB2 cannabinoid receptors are active, the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication.<br /> <br /> An inhibitor binds to the active site of the enzyme lowering the rate at which the enzyme degrades substrate, thus enzyme inhibitors are often used as drugs. A FAAH inhibitor offers great potential as a pain relief drug because FAAH commonly degrades anandamide. If the enzymatic activity of FAAH was lowered there would be increased levels of anandamide causing increased appetite, sleep, and pain relief.<br /> <br /> A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site.<ref name="Most Recent Study">PMID:23581831</ref> A humanized rat variant of FAAH was inhibited by BR1, CL, and PEG. The mice displayed an increase in endogenous brain levels of the FAAH substrate anandamide for over six hours.<ref name="Most Recent Study">PMID:23581831</ref> This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4J5P; K and L of 1MT5' scene='57/573135/4j5p_dimer/3'><br /> <br /> == Function ==<br /> The fatty acid amide hydrolase <scene name='57/573135/4j5p_dimer/3'>dimer</scene> is an integral membrane protein that cleaves fatty acid amides at the carbon-oxygen double bond in the amide functional group.<ref name="Wiki FAAH">http://en.wikipedia.org/wiki/FAAH</ref> <br /> <br /> [[Image:Anandamide.png|150 px|left|thumb|Figure 2: Anadamide, hydrolysis substrate of FAAH]]<br /> <br /> 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 <scene name='57/573135/Ser241_4j5p/1'>Ser241</scene>, 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 BR1 covalently binds to Ser241 disrupting the [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] active site and inactivating the [http://en.wikipedia.org/wiki/Hydrolase hydrolase].<ref name= "4HBP">PMID:23218778</ref> Without the active FAAH, anandamide accumulates, resulting in pain relief due to its increased concentration and interaction with the CB1 and CB2 cannabinoid receptors.<br /> <br /> ==Structure==<br /> The <scene name='57/573136/Starting_view/1'>surface</scene> of FAAH reveals two openings 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/4'>membrane access channels</scene> (MAC) are 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.<br /> <br /> <br /> <br /> </StructureSection><br /> <br /> <br /> <br /> <br /> == References ==<br /> <br /> <references/></div>

Daniel B. Lange https://proteopedia.org/index.php?title=File:Anandamide.png&diff=1918296 File:Anandamide.png 2014-04-25T11:43:03Z

<p>Daniel B. Lange: </p> <hr /> <div></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1918295 Sandbox Reserved 922 2014-04-25T11:39:37Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> 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 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.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1918294 Sandbox Reserved 922 2014-04-25T11:30:40Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> 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 <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 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.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1918293 Sandbox Reserved 922 2014-04-25T09:37:55Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> 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 <scene name='57/573136/Membrane_access_channel/11'>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 positively charged residues to lure out partitioned anandamide by its narrow partial negative charge. 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.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1918292 Sandbox Reserved 922 2014-04-25T09:31:54Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> 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 <scene name='57/573136/Membrane_access_channel/10'>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 positively charged residues to lure out partitioned anandamide by its narrow partial negative charge. 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.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1918291 Sandbox Reserved 922 2014-04-25T08:20:05Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> 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 that partially covers the entry way with Phe432. 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.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1918290 Sandbox Reserved 922 2014-04-25T06:39:30Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> 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.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1915387 Sandbox Reserved 922 2014-04-23T00:28:45Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> 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. <scene name='57/573136/Membrane_access_channel/9'>Flaps 1 and 2</scene> envelope the middle and backside of the anandamide mimic, and are locked together by a salt bridge between Arg486 and Asp403. 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.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1915382 Sandbox Reserved 922 2014-04-23T00:18:46Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> The <scene name='57/573136/Starting_view/1'>surface</scene> of FAAH reveals two 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/4'>membrane access channels</scene> (MAC) are made up of three flaps and two intrusions. <scene name='57/573136/Membrane_access_channel/9'>Flaps 1 and 2</scene> envelope the middle and backside of the anandamide mimic, and are locked together by a salt bridge between Arg486 and Asp403. 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.<br /> <br /> </StructureSection ><br /> <br /> <scene name='57/573136/Membrane_access_channel/8'>Membrane Access Channel</scene></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1915373 Sandbox Reserved 922 2014-04-22T22:35:33Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> The <scene name='57/573136/Starting_view/1'>surface</scene> of FAAH reveals two 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/4'>membrane access channels</scene> (MAC) are 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.<br /> <br /> </StructureSection ><br /> <br /> <scene name='57/573136/Membrane_access_channel/8'>Membrane Access Channel</scene></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1915303 Sandbox Reserved 922 2014-04-22T05:47:15Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> The <scene name='57/573136/Starting_view/1'>surface</scene> of FAAH reveals <scene name='57/573136/Starting_view/3'>two openings</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/4'>membrane access channels</scene> (MAC) are 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.<br /> <br /> </StructureSection ><br /> <br /> <scene name='57/573136/Membrane_access_channel/8'>Membrane Access Channel</scene></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1915302 Sandbox Reserved 922 2014-04-22T05:43:20Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <br /> The <scene name='57/573136/Starting_view/1'>surface</scene> of FAAH reveals <scene name='57/573136/Starting_view/2'>two openings</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/4'>membrane access channels</scene> (MAC) are 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.<br /> <br /> </StructureSection ><br /> <br /> <scene name='57/573136/Membrane_access_channel/8'>Membrane Access Channel</scene></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1915301 Sandbox Reserved 922 2014-04-22T05:00:41Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> </StructureSection ><br /> <br /> <scene name='57/573136/Membrane_access_channel/8'>Membrane Access Channel</scene></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1915300 Sandbox Reserved 922 2014-04-22T04:08:47Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> </StructureSection ><br /> <br /> <scene name='57/573136/Membrane_access_channel/6'>TextToBeDisplayed</scene></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1910004 Sandbox Reserved 921 2014-04-04T16:39:37Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Ser, Ser, Lys Catalytic Triad]]<br /> <br /> <br /> == Introduction ==<br /> Fatty acid amide hydrolase[http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides[http://en.wikipedia.org/wiki/Fatty_acid_amide]. FAAH is most commonly known for the degradation of anandamide[http://en.wikipedia.org/wiki/Anandamide], which is an endocannabinoid that activates the CB1 and CB2 cannabinoid receptors[http://en.wikipedia.org/wiki/Cannabinoid_receptor]. When CB1 and CB2 cannabinoid receptors are active the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication. A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site. A humanized rat variant of FAAH was inhibited and the mice displayed an increase in endogenous brain levels of FAAH substrates for over six hours. This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4J5P; K and L of 1MT5' scene='57/573135/4j5p_dimer/3'><br /> <br /> == Function ==<br /> The Fatty acid amide hydrolase <scene name='57/573135/4j5p_dimer/3'>dimer</scene> is an integral protein that 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 <scene name='57/573135/Ser241_4j5p/1'>Ser241</scene>, 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 accumulates, resulting in pain relief due to its interaction with the CB1 and CB2 cannabinoid receptors.<br /> <br /> ==Structure==<br /> The <scene name='57/573136/Starting_view/1'>surface</scene> of FAAH reveals two openings directly accessible by the inner layer of the lipid bilayer. These <scene name='57/573136/Membrane_access_channel/4'>membrane access channels</scene> (MAC) are each proceed by a respective membrane binding cap. This sturdy flap appears to be loosened by the presence of five positively charged residues, and the each MAC is remains conformation-stable by a salt bridge. The membrane access channel leads to the active site, which is flanked by the both the <scene name='57/573136/Cytosolic_port/2'>acyl chain binding pocket and cytosolic port </scene> (ABP and CP). The cytosolic port is a lengthy, flexible loop that leads directly into the cytoplasm, allowing the deacylated amine to enter the cell.<br /> <br /> <br /> <br /> </StructureSection><br /> <br /> <br /> <br /> <br /> == References ==<br /> <references/><br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1910001 Sandbox Reserved 921 2014-04-04T08:43:29Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Ser, Ser, Lys Catalytic Triad]]<br /> <br /> <br /> == Introduction ==<br /> Fatty acid amide hydrolase[http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides[http://en.wikipedia.org/wiki/Fatty_acid_amide]. FAAH is most commonly known for the degradation of anandamide[http://en.wikipedia.org/wiki/Anandamide], which is an endocannabinoid that activates the CB1 and CB2 cannabinoid receptors[http://en.wikipedia.org/wiki/Cannabinoid_receptor]. When CB1 and CB2 cannabinoid receptors are active the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication. A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site. A humanized rat variant of FAAH was inhibited and the mice displayed an increase in endogenous brain levels of FAAH substrates for over six hours. This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4J5P; K and L of 1MT5' scene='57/573135/4j5p_dimer/3'><br /> <br /> == Function ==<br /> The Fatty acid amide hydrolase <scene name='57/573135/4j5p_dimer/3'>dimer</scene> is an integral protein that 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 <scene name='57/573135/Ser241_4j5p/1'>Ser241</scene>, 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 accumulates, resulting in pain relief due to its interaction with the CB1 and CB2 cannabinoid receptors.<br /> <br /> ==Structure==<br /> The <scene name='57/573136/Starting_view/1'>surface</scene> of FAAH reveals two openings directly accessible by the inner layer of the lipid bilayer. These <scene name='57/573136/Membrane_access_channel/4'>membrane access channels</scene> (MAC) are each proceed by a respective membrane binding cap. This sturdy flap appears to be loosened by the presence of five positively charged residues, and the each MAC is remains conformation-stable by a salt bridge. The membrane access channel leads to the active site, which is flanked by the both the <scene name='57/573136/Cytosolic_port/2'>acyl chain binding pocket and cytosolic port </scene> (ABP and CP). The cytosolic port is a lengthy, flexible loop that leads directly into the cytoplasm, allowing the deacylated amine to enter the cell.<br /> <br /> <br /> <br /> </StructureSection><br /> <br /> <br /> <br /> <br /> == References ==<br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1910000 Sandbox Reserved 921 2014-04-04T08:38:48Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Ser, Ser, Lys Catalytic Triad]]<br /> <br /> <br /> == Introduction ==<br /> Fatty acid amide hydrolase[http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides[http://en.wikipedia.org/wiki/Fatty_acid_amide]. FAAH is most commonly known for the degradation of anandamide[http://en.wikipedia.org/wiki/Anandamide], which is an endocannabinoid that activates the CB1 and CB2 cannabinoid receptors[http://en.wikipedia.org/wiki/Cannabinoid_receptor]. When CB1 and CB2 cannabinoid receptors are active the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication. A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site. A humanized rat variant of FAAH was inhibited and the mice displayed an increase in endogenous brain levels of FAAH substrates for over six hours. This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4J5P; K and L of 1MT5' scene='57/573135/4j5p_dimer/3'><br /> <br /> == Function ==<br /> The Fatty acid amide hydrolase <scene name='57/573135/4j5p_dimer/3'>dimer</scene> is an integral protein that 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 <scene name='57/573135/Ser241_4j5p/1'>Ser241</scene>, 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 accumulates, resulting in pain relief due to its interaction with the CB1 and CB2 cannabinoid receptors.<br /> <br /> ==Structure==<br /> The <scene name='57/573136/Starting_view/1'>surface</scene> of FAAH reveals two openings directly accessible by the inner layer of the lipid bilayer. These <scene name='57/573136/Membrane_access_channel/4'>membrane access channels</scene> (MAC) are each proceed by a respective membrane binding cap. This sturdy flap appears to be loosened by the presence of five positively charged residues, and the each MAC is remains conformation-stable by a salt bridge. The membrane access channel leads to the active site, which is flanked by the both the <scene name='57/573136/Cytosolic_port/2'>acyl chain binding pocket and cytosolic port </scene> (ABP and CP). The cytosolic port is a lengthy, flexible loop that leads directly into the cytoplasm, allowing the deacylated amine to enter the cell.<br /> <br /> <br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><br /> <br /> <br /> </StructureSection><br /> <br /> <br /> <br /> <br /> == References ==<br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909999 Sandbox Reserved 921 2014-04-04T08:19:05Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Figure Legend]]<br /> <br /> <br /> == Introduction ==<br /> Fatty acid amide hydrolase[http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides[http://en.wikipedia.org/wiki/Fatty_acid_amide]. FAAH is most commonly known for the degradation of anandamide[http://en.wikipedia.org/wiki/Anandamide], which is an endocannabinoid that activates the CB1 and CB2 cannabinoid receptors[http://en.wikipedia.org/wiki/Cannabinoid_receptor]. When CB1 and CB2 cannabinoid receptors are active the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication. A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site. A humanized rat variant of FAAH was inhibited and the mice displayed an increase in endogenous brain levels of FAAH substrates for over six hours. This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4J5P; K and L of 1MT5' scene='57/573135/4j5p_dimer/3'><br /> <br /> == Function ==<br /> The Fatty acid amide hydrolase <scene name='57/573135/4j5p_dimer/3'>dimer</scene> 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 <scene name='57/573135/Ser241_4j5p/1'>Ser241</scene>, 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 accumulates, resulting in pain relief due to its interaction with the CB1 and CB2 cannabinoid receptors.<br /> <br /> <br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><br /> <br /> <br /> </StructureSection><br /> <br /> <br /> <br /> <br /> == References ==<br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909998 Sandbox Reserved 921 2014-04-04T08:18:02Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Figure Legend]]<br /> <br /> <br /> == Introduction ==<br /> Fatty acid amide hydrolase[http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides[http://en.wikipedia.org/wiki/Fatty_acid_amide]. FAAH is most commonly known for the degradation of anandamide[http://en.wikipedia.org/wiki/Anandamide], which is an endocannabinoid that activates the CB1 and CB2 cannabinoid receptors[http://en.wikipedia.org/wiki/Cannabinoid_receptor]. When CB1 and CB2 cannabinoid receptors are active the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication. A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site. A humanized rat variant of FAAH was inhibited and the mice displayed an increase in endogenous brain levels of FAAH substrates for over six hours. This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4HBP; K and L of 1MT5' scene='57/573135/Ser241_4j5p/1'><br /> <br /> == Function ==<br /> The Fatty acid amide hydrolase <scene name='57/573135/4j5p_dimer/3'>dimer</scene> 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 <scene name='57/573135/Ser241_4j5p/1'>Ser241</scene>, 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 accumulates, resulting in pain relief due to its interaction with the CB1 and CB2 cannabinoid receptors.<br /> <br /> <br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><br /> <br /> <br /> </StructureSection><br /> <br /> <br /> <br /> <br /> == References ==<br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909997 Sandbox Reserved 921 2014-04-04T08:12:43Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Figure Legend]]<br /> <br /> <br /> == Introduction ==<br /> Fatty acid amide hydrolase[http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides[http://en.wikipedia.org/wiki/Fatty_acid_amide]. FAAH is most commonly known for the degradation of anandamide[http://en.wikipedia.org/wiki/Anandamide], which is an endocannabinoid that activates the CB1 and CB2 cannabinoid receptors[http://en.wikipedia.org/wiki/Cannabinoid_receptor]. When CB1 and CB2 cannabinoid receptors are active the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication. A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site. A humanized rat variant of FAAH was inhibited and the mice displayed an increase in endogenous brain levels of FAAH substrates for over six hours. This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4HBP; K and L of 1MT5' scene='57/573135/Ser241_4j5p/1'><br /> <br /> == Function ==<br /> 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 <scene name='57/573135/Ser241_4j5p/1'>Ser241</scene>, 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 accumulates, resulting in pain relief due to its interaction with the CB1 and CB2 cannabinoid receptors.<br /> <br /> <br /> <scene name='57/573135/4j5p_dimer/3'>Dimer</scene><br /> <br /> <br /> <br /> 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>.<br /> <br /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><br /> <br /> <br /> </StructureSection><br /> <br /> <br /> <br /> <br /> == References ==<br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909996 Sandbox Reserved 921 2014-04-04T08:12:05Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Figure Legend]]<br /> <br /> <br /> == Introduction ==<br /> Fatty acid amide hydrolase[http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides[http://en.wikipedia.org/wiki/Fatty_acid_amide]. FAAH is most commonly known for the degradation of anandamide[http://en.wikipedia.org/wiki/Anandamide], which is an endocannabinoid that activates the CB1 and CB2 cannabinoid receptors[http://en.wikipedia.org/wiki/Cannabinoid_receptor]. When CB1 and CB2 cannabinoid receptors are active the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication. A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site. A humanized rat variant of FAAH was inhibited and the mice displayed an increase in endogenous brain levels of FAAH substrates for over six hours. This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4HBP; K and L of 1MT5' scene='57/573135/Ser241_4j5p/1'><br /> <br /> == Function ==<br /> 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 <scene name='57/573135/Ser241_4j5p/1'>Ser241 bound to ligand</scene>, 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 accumulates, resulting in pain relief due to its interaction with the CB1 and CB2 cannabinoid receptors.<br /> <br /> <br /> <scene name='57/573135/4j5p_dimer/3'>Dimer</scene><br /> <br /> <br /> <br /> 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>.<br /> <br /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><br /> <br /> <br /> </StructureSection><br /> <br /> <br /> <br /> <br /> == References ==<br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909995 Sandbox Reserved 921 2014-04-04T08:07:37Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Figure Legend]]<br /> <br /> <br /> == Introduction ==<br /> Fatty acid amide hydrolase[http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides[http://en.wikipedia.org/wiki/Fatty_acid_amide]. FAAH is most commonly known for the degradation of anandamide[http://en.wikipedia.org/wiki/Anandamide], which is an endocannabinoid that activates the CB1 and CB2 cannabinoid receptors[http://en.wikipedia.org/wiki/Cannabinoid_receptor]. When CB1 and CB2 cannabinoid receptors are active the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication. A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site. A humanized rat variant of FAAH was inhibited and the mice displayed an increase in endogenous brain levels of FAAH substrates for over six hours. This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4HBP; K and L of 1MT5' scene='57/573135/Ser241_4j5p/1'><br /> <br /> == Function ==<br /> 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.<br /> <br /> <scene name='57/573135/Ser241_4j5p/1'>Ser241 bound to ligand</scene><br /> <scene name='57/573135/4j5p_dimer/3'>Dimer</scene><br /> <br /> <br /> <br /> 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>.<br /> <br /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><br /> <br /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> 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.<br /> <br /> <br /> == References ==<br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909994 Sandbox Reserved 921 2014-04-04T08:06:18Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Figure Legend]]<br /> <br /> <br /> == Introduction ==<br /> Fatty acid amide hydrolase[http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides[http://en.wikipedia.org/wiki/Fatty_acid_amide]. FAAH is most commonly known for the degradation of anandamide[http://en.wikipedia.org/wiki/Anandamide], which is an endocannabinoid that activates the CB1 and CB2 cannabinoid receptors[http://en.wikipedia.org/wiki/Cannabinoid_receptor]. When CB1 and CB2 cannabinoid receptors are active the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication. A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site. A humanized rat variant of FAAH was inhibited and the mice displayed an increase in endogenous brain levels of FAAH substrates for over six hours. This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='4HBP; K and L of 1MT5' scene='57/573135/Ser241_4j5p/1'><br /> <scene name='57/573135/Ser241_4j5p/1'>Ser241 bound to ligand</scene><br /> <scene name='57/573135/4j5p_dimer/3'>Dimer</scene><br /> <br /> <scene name='57/573135/Catalytic_triad/2'>Catalytic Triad</scene><br /> <br /> 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>.<br /> <br /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><br /> <br /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> 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.<br /> <br /> <br /> == References ==<br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909993 Sandbox Reserved 921 2014-04-04T07:51:23Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> '''Fatty Acid Amide Hydrolase'''<br /> <br /> [[Image:CatalyticTriadProteopedia.png|100 px|left|thumb|Figure Legend]]<br /> <br /> <br /> == Introduction ==<br /> Fatty acid amid hydrolase[http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides[http://en.wikipedia.org/wiki/Fatty_acid_amide]. FAAH is most commonly known for the degradation of anandamid[http://en.wikipedia.org/wiki/Anandamide], which is an endocannabinoid that activates the CB1 and CB2 cannabinoid receptors[http://en.wikipedia.org/wiki/Cannabinoid_receptor]. When CB1 and CB2 cannabinoid receptors are active the receptors affect appetite, sleep, and relief of pain. The ability to inhibit FAAH has been widely investigated for possible pain relief medication. A recent study on FAAH inhibitors combined an irreversible bond at Cys269 and a reversible bond at Ser241 of the active site. A humanized rat variant of FAAH was inhibited and the mice displayed an increase in endogenous brain levels of FAAH substrates for over six hours. This is the first step towards developing a long lasting pain relief medication by inhibiting FAAH. <br /> <br /> <StructureSection load='4J5P' size='340' side='right' caption='FAAH' scene='57/573135/Ser241_4j5p/1'><br /> <scene name='57/573135/Ser241_4j5p/1'>Ser241 bound to ligand</scene><br /> <scene name='57/573135/4j5p_dimer/3'>Dimer</scene><br /> <br /> <scene name='57/573135/Catalytic_triad/2'>Catalytic Triad</scene><br /> <br /> 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>.<br /> <br /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><br /> <br /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> The fatty acid amide hydrolase cleaves fatty acid amides at the carbon-oxygen double bond in the amide functional group. FAAH uses the active site a catalytic triad consisting of Ser241, Ser217, and Lys142 to degrade the lipids. 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.<br /> <br /> <br /> == References ==<br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909992 Sandbox Reserved 922 2014-04-04T07:47:00Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909991 Sandbox Reserved 922 2014-04-04T07:43:24Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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/1'>Acyl Binding Pocket and Cytosolic Port</scene><br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909990 Sandbox Reserved 922 2014-04-04T05:55:54Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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>.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909989 Sandbox Reserved 922 2014-04-04T05:48:14Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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/3'>Membrane Access Channel (MAC)</scene>.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909988 Sandbox Reserved 922 2014-04-04T05:44:23Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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/2'>Membrane Access Channel (MAC)</scene>.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909987 Sandbox Reserved 922 2014-04-04T05:40:52Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/2' ><br /> <br /> <br /> <br /> <br /> 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/1'>Membrane Access Channel (MAC)</scene>.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909986 Sandbox Reserved 922 2014-04-04T05:29:58Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/1' ><br /> <br /> <br /> <br /> <br /> 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/1'>Membrane Access Channel (MAC)</scene>.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909985 Sandbox Reserved 922 2014-04-04T05:28:46Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/1' ><br /> <br /> This is the <scene name='57/573136/Membrane_access_channel/1'>Membrane Access Channel (MAC)</scene>.<br /> <br /> <br /> 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.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909960 Sandbox Reserved 922 2014-04-04T02:12:58Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/1' ><br /> <br /> 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.<br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909959 Sandbox Reserved 922 2014-04-04T02:11:05Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Chains K and L from 1MT5' scene='57/573136/Starting_view/1' ><br /> <br /> This is the overall <scene name='57/573136/Starting_view/1'>TextToBeDisplayed</scene>. <br /> <br /> </StructureSection ><br /> <br /> <br /> <br /> <scene name='57/573136/Starting_view/1'>TextToBeDisplayed</scene><br /> <br /> <br /> <scene name='57/573136/Faah_dimer/4'>Far Out View</scene>;<br /> <scene name='57/573136/Faah_dimer/5'>Approach</scene><br /> <br /> <scene name='57/573136/Starting_view/1'>TextToBeDisplayed</scene></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909958 Sandbox Reserved 922 2014-04-04T02:07:06Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Anionic Hole' scene='57/573136/Starting_view/1' ><br /> <br /> <br /> <br /> </StructureSection ><br /> <br /> <br /> <br /> <scene name='57/573136/Starting_view/1'>TextToBeDisplayed</scene><br /> <br /> <br /> <scene name='57/573136/Faah_dimer/4'>Far Out View</scene>;<br /> <scene name='57/573136/Faah_dimer/5'>Approach</scene><br /> <br /> <scene name='57/573136/Starting_view/1'>TextToBeDisplayed</scene></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909951 Sandbox Reserved 922 2014-04-04T01:56:34Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='1MT5' size='350' frame='true' align='right' caption='Anionic Hole' scene='57/573136/Faah_dimer/4' ><br /> <br /> <br /> <scene name='57/573136/Faah_dimer/4'>Far Out View</scene>;<br /> <scene name='57/573136/Faah_dimer/5'>Approach</scene><br /> <br /> <br /> </StructureSection ><br /> <br /> <Structure load='FAAH_dimer.pdb' size='350' frame='true' align='right' caption='Insert caption here' scene='57/573136/Starting_view/1' /><br /> <br /> <scene name='57/573136/Starting_view/1'>TextToBeDisplayed</scene></div>

Daniel B. Lange https://proteopedia.org/index.php?title=File:FAAH_dimer.pdb&diff=1909940 File:FAAH dimer.pdb 2014-04-04T01:30:00Z

<p>Daniel B. Lange: uploaded a new version of "Image:FAAH dimer.pdb"</p> <hr /> <div></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909920 Sandbox Reserved 922 2014-04-03T23:23:26Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='1MT5' size='350' frame='true' align='right' caption='Anionic Hole' scene='57/573136/Faah_dimer/4' ><br /> <br /> <br /> <scene name='57/573136/Faah_dimer/4'>Far Out View</scene>;<br /> <scene name='57/573136/Faah_dimer/5'>Approach</scene><br /> <br /> <br /> </StructureSection ><br /> <br /> <Structure load='4HBP' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1909919 Sandbox Reserved 922 2014-04-03T23:21:42Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='1MT5' size='350' frame='true' align='right' caption='Anionic Hole' scene='57/573136/Faah_dimer/4' ><br /> <Structure load='4HBP' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><br /> <br /> <br /> <scene name='57/573136/Faah_dimer/4'>Far Out View</scene>;<br /> <scene name='57/573136/Faah_dimer/5'>Approach</scene><br /> <br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1907493 Sandbox Reserved 922 2014-03-28T18:27:26Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='1MT5' size='350' frame='true' align='right' caption='Anionic Hole' scene='57/573136/Faah_dimer/4' ><br /> <br /> <scene name='57/573136/Faah_dimer/4'>Far Out View</scene>;<br /> <scene name='57/573136/Faah_dimer/5'>Approach</scene><br /> <br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1907490 Sandbox Reserved 922 2014-03-28T18:22:18Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='1MT5' size='350' frame='true' align='right' caption='Anionic Hole' scene='57/573136/Faah_dimer/4' ><br /> <br /> <scene name='57/573136/Faah_dimer/4'>Far Out View</scene><br /> <scene name='57/573136/Faah_dimer/5'>Approach</scene><br /> <br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1907489 Sandbox Reserved 922 2014-03-28T18:21:04Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='1MT5' size='350' frame='true' align='right' caption='Anionic Hole' scene='57/573136/Faah_dimer/4' ><br /> <br /> <br /> <scene name='57/573136/Faah_dimer/5'>Approach</scene><br /> <br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1907487 Sandbox Reserved 922 2014-03-28T18:20:24Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='1MT5' size='350' frame='true' align='right' caption='Anionic Hole' scene='57/573136/Faah_dimer/4' ><br /> <br /> <br /> <scene name='57/573136/Faah_dimer/5'></scene><br /> <br /> <br /> </StructureSection ></div>

Daniel B. Lange https://proteopedia.org/index.php?title=Sandbox_Reserved_922&diff=1907466 Sandbox Reserved 922 2014-03-28T17:57:28Z

<p>Daniel B. Lange: </p> <hr /> <div><br /> {{Johnson_CH462_Spring2014}}<br /> <br /> <br /> <StructureSection load='1MT5' size='350' frame='true' align='right' caption='Anionic Hole' scene='57/573136/Faah_dimer/4' ><br /> <br /> <scene name='57/573136/Faah_dimer/4'>TextToBeDisplayed</scene><br /> <br /> <br /> </StructureSection ></div>

Daniel B. Lange