Structural Adaptations in a Membrane Enzyme That Terminates Endocannabinoid Signaling

• DOI: 10.1126/science.1076535
• Publication Date: 2002-11-29T15:32:06Z
• Authors: Michael H. Bracey; Michael A. Hanson; Kim R. Masuda; Raymond C. Stevens; Benjamin F. Cravatt
• Keywords: Second messenger system; Hydrolase; Cell Signaling

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