Sandbox Reserved 911: Difference between revisions

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Crystal structures of FAAH show that the enzyme is a <scene name='57/573125/2vya/1'>homodimer</scene> with <scene name='57/573125/2vya/3'>PF-750 inhibitor</scene> in solution, with each subunit having a mass of 63 kD. The protein's <scene name='57/573125/2vya/8'>twisted Beta sheet core</scene> of 11 strands is surrounded by 24 alpha helices. The enzyme is embedded in the cell <scene name='57/573125/2vya/5'>membrane</scene> to catch the lipid signaling molecules that can diffuse through membranes. The FAAH structure shows an entry channel leading from the lipid bilayer to the enzyme's active site, providing a path for endocannabinoids to enter the hydrolase. In addition, FAAH possesses a channel leading from the active site to the cell's cytoplasm, allowing the release of polar compounds released from lipid cleavage and the entry of water molecules necessary for the FAAH mechanism to proceed. (IMT5)

This hydrolase has a membrane binding cap, a <scene name='57/573125/2vya/7'>helix-turn-helix motif</scene> consisting of alpha helices 18 and 19. These helices present hydrophobic amino acid residues that ~~likely~~ help FAAH interact with the hydrophobic region of the lipid bilayer. (IMT5)

This hydrolase has a membrane binding cap, a <scene name='57/573125/2vya/7'>helix-turn-helix motif</scene> consisting of alpha helices 18 and 19. These helices present hydrophobic amino acid residues that help FAAH interact with the hydrophobic region of the lipid bilayer. (IMT5)

Sandbox Reserved 911: Difference between revisions

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Revision as of 13:16, 25 March 2014 view source Rachel Erkilla (talk \| contribs) 92 edits No edit summary ← Older edit		Revision as of 13:23, 25 March 2014 view source Rachel Erkilla (talk \| contribs) 92 edits No edit summary Newer edit →
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	Crystal structures of FAAH show that the enzyme is a <scene name='57/573125/2vya/1'>homodimer</scene> with <scene name='57/573125/2vya/3'>PF-750 inhibitor</scene> in solution, with each subunit having a mass of 63 kD. The protein's <scene name='57/573125/2vya/8'>twisted Beta sheet core</scene> of 11 strands is surrounded by 24 alpha helices. The enzyme is embedded in the cell <scene name='57/573125/2vya/5'>membrane</scene> to catch the lipid signaling molecules that can diffuse through membranes. The FAAH structure shows an entry channel leading from the lipid bilayer to the enzyme's active site, providing a path for endocannabinoids to enter the hydrolase. In addition, FAAH possesses a channel leading from the active site to the cell's cytoplasm, allowing the release of polar compounds released from lipid cleavage and the entry of water molecules necessary for the FAAH mechanism to proceed. (IMT5)		Crystal structures of FAAH show that the enzyme is a <scene name='57/573125/2vya/1'>homodimer</scene> with <scene name='57/573125/2vya/3'>PF-750 inhibitor</scene> in solution, with each subunit having a mass of 63 kD. The protein's <scene name='57/573125/2vya/8'>twisted Beta sheet core</scene> of 11 strands is surrounded by 24 alpha helices. The enzyme is embedded in the cell <scene name='57/573125/2vya/5'>membrane</scene> to catch the lipid signaling molecules that can diffuse through membranes. The FAAH structure shows an entry channel leading from the lipid bilayer to the enzyme's active site, providing a path for endocannabinoids to enter the hydrolase. In addition, FAAH possesses a channel leading from the active site to the cell's cytoplasm, allowing the release of polar compounds released from lipid cleavage and the entry of water molecules necessary for the FAAH mechanism to proceed. (IMT5)

	This hydrolase has a membrane binding cap, a <scene name='57/573125/2vya/7'>helix-turn-helix motif</scene> consisting of alpha helices 18 and 19. These helices present hydrophobic amino acid residues that ~~likely~~ help FAAH interact with the hydrophobic region of the lipid bilayer. (IMT5)		This hydrolase has a membrane binding cap, a <scene name='57/573125/2vya/7'>helix-turn-helix motif</scene> consisting of alpha helices 18 and 19. These helices present hydrophobic amino acid residues that help FAAH interact with the hydrophobic region of the lipid bilayer. (IMT5)