3qk5: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qk5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qk5 RCSB], [http://www.ebi.ac.uk/pdbsum/3qk5 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qk5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qk5 RCSB], [http://www.ebi.ac.uk/pdbsum/3qk5 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/FAAH1_RAT FAAH1_RAT]] Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates (By similarity). | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 16:17, 25 December 2014
Crystal structure of fatty acid amide hydrolase with small molecule inhibitorCrystal structure of fatty acid amide hydrolase with small molecule inhibitor
Structural highlights
Function[FAAH1_RAT] Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates (By similarity). Publication Abstract from PubMedStarting from a series of ureas that were determined to be mechanism-based inhibitors of FAAH, several spirocyclic ureas and lactams were designed and synthesized. These efforts identified a series of novel, noncovalent FAAH inhibitors with in vitro potency comparable to known covalent FAAH inhibitors. The mechanism of action for these compounds was determined through a combination of SAR and co-crystallography with rat FAAH. Identification of potent, noncovalent fatty acid amide hydrolase (FAAH) inhibitors.,Gustin DJ, Ma Z, Min X, Li Y, Hedberg C, Guimaraes C, Porter AC, Lindstrom M, Lester-Zeiner D, Xu G, Carlson TJ, Xiao S, Meleza C, Connors R, Wang Z, Kayser F Bioorg Med Chem Lett. 2011 Apr 15;21(8):2492-6. Epub 2011 Feb 17. PMID:21392988[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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