Proteopedia - User contributions [en]

https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Carter+Sharp Proteopedia - User contributions [en] 2026-09-15T09:37:30Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1915379 Sandbox Reserved 921 2014-04-23T00:10:35Z

<p>Carter Sharp: </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> 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>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1915378 Sandbox Reserved 921 2014-04-23T00:09:35Z

<p>Carter Sharp: </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 /> 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 /> 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> 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>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1915377 Sandbox Reserved 921 2014-04-23T00:05:34Z

<p>Carter Sharp: </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 /> 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 /> 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. 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>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1915374 Sandbox Reserved 921 2014-04-22T23:31:59Z

<p>Carter Sharp: </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 is most commonly known for the degradation of [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. 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 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 [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] active site and leaving the [http://en.wikipedia.org/wiki/Hydrolase hydrolase] inactive.<ref name= "4HBP">PMID:23218778</ref> 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 [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>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1910014 Sandbox Reserved 921 2014-04-04T18:23:57Z

<p>Carter Sharp: </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 /> [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 is most commonly known for the degradation of [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. 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 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 [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] active site and leaving the [http://en.wikipedia.org/wiki/Hydrolase hydrolase] inactive.<ref name= "4HBP">PMID:23218778</ref> 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 [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>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1910013 Sandbox Reserved 921 2014-04-04T18:23:09Z

<p>Carter Sharp: </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 /> [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 is most commonly known for the degradation of [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. 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 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 [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] active site and leaving the [http://en.wikipedia.org/wiki/Hydrolase hydrolase] inactive.<ref name= "4HBP">PMID:23218778</ref> 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 [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 /> <ref name="Most Recent Study"/><br /> <references/></div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1910012 Sandbox Reserved 921 2014-04-04T18:16:35Z

<p>Carter Sharp: </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 /> [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 is most commonly known for the degradation of [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. 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 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 [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] active site and leaving the [http://en.wikipedia.org/wiki/Hydrolase 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 [http://en.wikipedia.org/wiki/Lipid_bilayer 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 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). 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 /> <ref name="Most Recent Study"/><br /> <references/></div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1910011 Sandbox Reserved 921 2014-04-04T18:14:45Z

<p>Carter Sharp: </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 /> [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 is most commonly known for the degradation of [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. 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 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[http://en.wikipedia.org/wiki/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 [http://en.wikipedia.org/wiki/Lipid_bilayer 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 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). 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 /> <ref name="Most Recent Study"/><br /> <references/></div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1910010 Sandbox Reserved 921 2014-04-04T18:06:47Z

<p>Carter Sharp: </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 /> [http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase 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.<ref name="Most Recent Study">PMID:23581831</ref> 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[http://en.wikipedia.org/wiki/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 name="Most Recent Study"/><br /> <references/><br /> <br /> <br /> == External Resources ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1910009 Sandbox Reserved 921 2014-04-04T18:05:40Z

<p>Carter Sharp: </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 /> [http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase 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.<ref>PMID:23581831</ref> 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[http://en.wikipedia.org/wiki/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 /> <ref name="Most Recent Study">PMID:23581831</ref><br /> <ref name="Most Recent Study"/><br /> <references/><br /> <br /> <br /> == External Resources ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1910008 Sandbox Reserved 921 2014-04-04T18:01:05Z

<p>Carter Sharp: </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.<ref>PMID:23581831</ref> 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[http://en.wikipedia.org/wiki/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 /> <ref>PMID:23581831</ref><br /> <references/><br /> <br /> <br /> == External Resources ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909984 Sandbox Reserved 921 2014-04-04T04:41:31Z

<p>Carter Sharp: </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 /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><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>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909983 Sandbox Reserved 921 2014-04-04T04:34:56Z

<p>Carter Sharp: </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. 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 /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><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>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909982 Sandbox Reserved 921 2014-04-04T04:34:29Z

<p>Carter Sharp: </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 hydrolasehttp://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase] (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. 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 /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><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>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909981 Sandbox Reserved 921 2014-04-04T04:34:04Z

<p>Carter Sharp: </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. 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 /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><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>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909980 Sandbox Reserved 921 2014-04-04T04:22:21Z

<p>Carter Sharp: </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 (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. 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 /> <scene name='57/573136/Starting_view/1'>3D Structure</scene><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>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909979 Sandbox Reserved 921 2014-04-04T04:18:54Z

<p>Carter Sharp: </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 (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. 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 /> <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>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909978 Sandbox Reserved 921 2014-04-04T04:06:46Z

<p>Carter Sharp: </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 (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. 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 /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> <br /> == References ==<br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909977 Sandbox Reserved 921 2014-04-04T03:53:42Z

<p>Carter Sharp: </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 (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. 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 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 /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> <br /> == References ==<br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909976 Sandbox Reserved 921 2014-04-04T03:45:47Z

<p>Carter Sharp: </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 (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. 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[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 /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> <br /> == References ==<br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909975 Sandbox Reserved 921 2014-04-04T03:43:18Z

<p>Carter Sharp: </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 (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. 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[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 /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> <br /> == References ==<br /> <br /> <references/><br /> <ref>PMID:23581831</ref><br /> <br /> == External Resources ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909974 Sandbox Reserved 921 2014-04-04T03:40:49Z

<p>Carter Sharp: </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 (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. 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[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 /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> <br /> == References ==<br /> <references/><br /> <br /> <ref>PMID:23581831</ref><br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909973 Sandbox Reserved 921 2014-04-04T03:16:11Z

<p>Carter Sharp: </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 (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. 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[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 /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> <br /> == References ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909972 Sandbox Reserved 921 2014-04-04T03:15:43Z

<p>Carter Sharp: </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 (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. 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 [receptorshttp://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 /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> <br /> == References ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909971 Sandbox Reserved 921 2014-04-04T03:12:36Z

<p>Carter Sharp: </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 (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. 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. 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 /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> <br /> == References ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909970 Sandbox Reserved 921 2014-04-04T03:11:26Z

<p>Carter Sharp: </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 (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. FAAH is most commonly known for the degradation of [anandamide], which is an endocannabinoid that activates the CB1 and CB2 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. 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 /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> <br /> == References ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909969 Sandbox Reserved 921 2014-04-04T03:10:16Z

<p>Carter Sharp: </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 (FAAH) is the primary catabolic enzyme for the degradation of fatty acid amides. FAAH is most commonly known for the degradation of anandamide, which is an endocannabinoid that activates the CB1 and CB2 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. 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 /> <br /> </StructureSection><br /> <br /> <br /> == Function ==<br /> <br /> == References ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909964 Sandbox Reserved 921 2014-04-04T02:18:29Z

<p>Carter Sharp: </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 /> <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 /> <br /> </StructureSection><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909963 Sandbox Reserved 921 2014-04-04T02:17:49Z

<p>Carter Sharp: </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 /> <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 /> <br /> </StructureSection><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909962 Sandbox Reserved 921 2014-04-04T02:14:04Z

<p>Carter Sharp: </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 /> <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 /> <br /> </StructureSection><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909961 Sandbox Reserved 921 2014-04-04T02:13:42Z

<p>Carter Sharp: </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 /> <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 /> <br /> </StructureSection><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909957 Sandbox Reserved 921 2014-04-04T02:04:02Z

<p>Carter Sharp: </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 /> <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 /> <br /> </StructureSection><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909956 Sandbox Reserved 921 2014-04-04T02:01:25Z

<p>Carter Sharp: </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 /> <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 /> <br /> </StructureSection><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909955 Sandbox Reserved 921 2014-04-04T02:01:06Z

<p>Carter Sharp: </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 /> <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 /> <br /> </StuctureSection ><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909954 Sandbox Reserved 921 2014-04-04T02:00:07Z

<p>Carter Sharp: </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 /> <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 /> <br /> </StuctureSection><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909952 Sandbox Reserved 921 2014-04-04T01:56:37Z

<p>Carter Sharp: </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 /> <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 /> <br /> /<StuctureSection><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909950 Sandbox Reserved 921 2014-04-04T01:56:15Z

<p>Carter Sharp: </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 /> <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 /> <br /> <StuctureSection><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909949 Sandbox Reserved 921 2014-04-04T01:56:09Z

<p>Carter Sharp: </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 /> <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 /> <br /> <StuctureSection><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909948 Sandbox Reserved 921 2014-04-04T01:55:42Z

<p>Carter Sharp: </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 /> <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 /> <br /> </StuctureSection><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909946 Sandbox Reserved 921 2014-04-04T01:52:43Z

<p>Carter Sharp: </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 /> <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 /> <br /> </StuctureSection><br /> <br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909945 Sandbox Reserved 921 2014-04-04T01:49:05Z

<p>Carter Sharp: </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 /> <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 /> <br /> == Contents ==<br /> <br /> == Introduction ==<br /> <br /> == Headline text ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909944 Sandbox Reserved 921 2014-04-04T01:48:04Z

<p>Carter Sharp: </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 /> <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 /> <br /> == Contents ==</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909943 Sandbox Reserved 921 2014-04-04T01:47:23Z

<p>Carter Sharp: </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 /> <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 /> =<br /> == Contents ==<br /> =</div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909942 Sandbox Reserved 921 2014-04-04T01:46:25Z

<p>Carter Sharp: </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 /> <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></div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909941 Sandbox Reserved 921 2014-04-04T01:45:25Z

<p>Carter Sharp: </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 /> <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 /> <scene name='57/573135/Catalytic_triad/2'>Catalytic Triad</scene></div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909939 Sandbox Reserved 921 2014-04-04T00:31:17Z

<p>Carter Sharp: </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 /> <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></div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909938 Sandbox Reserved 921 2014-04-04T00:30:21Z

<p>Carter Sharp: </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 /> <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 /> <br /> <StructureSection load='4J5P' size='340' frame='true' align='right' caption='Dimer' scene='57/573135/4j5p_dimer/3'/><br /> <scene name='57/573135/4j5p_dimer/3'>TextToBeDisplayed</scene></div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909937 Sandbox Reserved 921 2014-04-04T00:29:52Z

<p>Carter Sharp: </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 /> <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 /> <br /> </StructureSection load='4J5P' size='340' frame='true' align='right' caption='Dimer' scene='57/573135/4j5p_dimer/3'/><br /> <scene name='57/573135/4j5p_dimer/3'>TextToBeDisplayed</scene></div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909936 Sandbox Reserved 921 2014-04-04T00:27:49Z

<p>Carter Sharp: </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 /> <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 /> <br /> </Structure load='4J5P' size='340' frame='true' align='right' caption='Dimer' scene='57/573135/4j5p_dimer/3'/></div>

Carter Sharp https://proteopedia.org/index.php?title=Sandbox_Reserved_921&diff=1909935 Sandbox Reserved 921 2014-04-04T00:26:50Z

<p>Carter Sharp: </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 /> <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 /> <br /> </Structure load='4J5P' size='340' frame='true' align='right' caption='Dimer' scene='57/573135/4j5p_dimer/3' /></div>

Carter Sharp