RGD Reference Report - Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling. - Rat Genome Database

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Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling.

Authors: Bracey, MH  Hanson, MA  Masuda, KR  Stevens, RC  Cravatt, BF 
Citation: Bracey MH, etal., Science 2002 Nov 29;298(5599):1793-6.
RGD ID: 728491
Pubmed: PMID:12459591   (View Abstract at PubMed)
DOI: DOI:10.1126/science.1076535   (Journal Full-text)

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.



Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
FaahRatidentical protein binding  IPIFaah (Rattus norvegicus)homodimerizationRGD 

Objects Annotated

Genes (Rattus norvegicus)
Faah  (fatty acid amide hydrolase)


Additional Information