1mt5
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CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE
OverviewOverview
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.
About this StructureAbout this Structure
1MT5 is a Single protein structure of sequence from Rattus norvegicus with MAY as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling., Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF, Science. 2002 Nov 29;298(5599):1793-6. PMID:12459591
Page seeded by OCA on Tue Nov 20 21:40:49 2007