PDB 4DO3 deposited: 2012-02-09 modified: 2013-01-23
Title Structure of FAAH with a non-steroidal anti-inflammatory drug
Authors Albani, C., Bertolacci, L., Cavalli, A., De Vivo, M., Dionisi, M., Garau, G., Lambruschini, C., Magotti, P., Piomelli, D., Romeo, E., Scarpelli, R., Veronesi, M.
Structure factors resolution 2.25 rfactor 0.16439 rfree 0.19872
DPI 0.43 theoretical min: 0.21

In addition to inhibiting the cyclooxygenase (COX)-mediated biosynthesis of prostanoids, various widely used nonsteroidal anti-inflammatory drugs (NSAIDs) enhance endocannabinoid signaling by blocking the anandamide-degrading membrane enzyme fatty acid amide hydrolase (FAAH). The X-ray structure of FAAH in complex with the NSAID carprofen, along with site-directed mutagenesis, enzyme activity assays, and NMR analysis, has revealed the molecular details of this interaction, providing information that may guide the design of dual FAAH-COX inhibitors with superior analgesic efficacy.

J.Am.Chem.Soc. 2013 Jan; 135(1):22-25 doi:10.1021/ja308733u

Cross References
Database source Identifier Description
PubMed 23240907 JACSAT
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
4DO3/1 4DO3 1 dimer 0 2 5 7020