Summary
PDB 1MT5 deposited: 2002-09-20 modified: 2009-02-24
Title CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE
Authors Bracey, M.H., Cravatt, B.F., Hanson, M.A., Masuda, K.R., Stevens, R.C.
Method X-RAY DIFFRACTION
Structure factors resolution None rfactor None rfree None
DPI
Citations

Cellular communication in the nervous system is mediated by chemical messengers that include amino acids, monoamines, peptide hormones, and lipids. An interesting question is how neurons regulate signals that are transmitted by membrane-embedded lipids. Here, we report the 2.8 angstrom crystal structure of the integral membrane protein fatty acid amide hydrolase (FAAH), an enzyme that degrades members of the endocannabinoid class of signaling lipids and terminates their activity. The structure of FAAH complexed with an arachidonyl inhibitor reveals how a set of discrete structural alterations allows this enzyme, in contrast to soluble hydrolases of the same family, to integrate into cell membranes and establish direct access to the bilayer from its active site.

science 2002 Nov; 298(5599):1793-1796 doi:10.1126/science.1076535

Cross References
Database source Identifier Description
PubMed 12459591 SCIEAS
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1MT5/1 1MT5 1 dimer 0 2 2 6162
1MT5/2 1MT5 2 dimer 0 2 2 6266
1MT5/3 1MT5 3 dimer 0 2 2 6302
1MT5/4 1MT5 4 dimer 0 2 2 6246
1MT5/5 1MT5 5 dimer 0 2 2 6251
1MT5/6 1MT5 6 dimer 0 2 2 6326
1MT5/7 1MT5 7 dimer 0 2 2 6263
1MT5/8 1MT5 8 dimer 0 2 2 6303