Summary
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.
Method X-RAY DIFFRACTION
Structure factors resolution 2.25 rfactor 0.16439 rfree 0.19872
DPI 0.43 theoretical min: 0.21
Citations

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