1MT5

CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE

1MT5 の概要

• エントリーDOI: 10.2210/pdb1mt5/pdb
• 分子名称: Fatty-acid amide hydrolase, METHYL ARACHIDONYL FLUOROPHOSPHONATE (2 entities in total)
• 機能のキーワード: amidase signature, hydrolase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Endoplasmic reticulum membrane; Single-pass membrane protein: P97612
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 949016.21

構造登録者

Bracey, M.H.,Hanson, M.A.,Masuda, K.R.,Stevens, R.C.,Cravatt, B.F. (登録日: 2002-09-20, 公開日: 2002-12-18, 最終更新日: 2024-10-16)

主引用文献

Bracey, M.H.,Hanson, M.A.,Masuda, K.R.,Stevens, R.C.,Cravatt, B.F.
Structural Adaptations in a Membrane Enzyme That Terminates Endocannabinoid Signaling
science, 298:1793-1796, 2002

PubMed Abstract: 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.

PubMed: 12459591
DOI: 10.1126/science.1076535

実験手法

X-RAY DIFFRACTION (2.8 Å)