3NKN

Crystal structure of mouse autotaxin in complex with 14:0-LPA

3NKN の概要

• エントリーDOI: 10.2210/pdb3nkn/pdb
• 関連するPDBエントリー: 3NKM 3NKO 3NKP 3NKQ 3NKR
• 分子名称: Ectonucleotide pyrophosphatase/phosphodiesterase family member 2, 1,2-ETHANEDIOL, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total)
• 機能のキーワード: lysophospholipase d, autotaxin, enpp2, lysophosphatidic acid, hydrolase
• 由来する生物種: Mus musculus (mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 100096.63

構造登録者

Nishimasu, H.,Ishitani, R.,Mihara, E.,Takagi, J.,Aoki, J.,Nureki, O. (登録日: 2010-06-20, 公開日: 2011-01-19, 最終更新日: 2024-11-13)

主引用文献

Nishimasu, H.,Okudaira, S.,Hama, K.,Mihara, E.,Dohmae, N.,Inoue, A.,Ishitani, R.,Takagi, J.,Aoki, J.,Nureki, O.
Crystal structure of autotaxin and insight into GPCR activation by lipid mediators
Nat.Struct.Mol.Biol., 18:205-212, 2011

PubMed Abstract: Autotaxin (ATX, also known as Enpp2) is a secreted lysophospholipase D that hydrolyzes lysophosphatidylcholine to generate lysophosphatidic acid (LPA), a lipid mediator that activates G protein-coupled receptors to evoke various cellular responses. Here, we report the crystal structures of mouse ATX alone and in complex with LPAs with different acyl-chain lengths and saturations. These structures reveal that the multidomain architecture helps to maintain the structural rigidity of the lipid-binding pocket, which accommodates the respective LPA molecules in distinct conformations. They indicate that a loop region in the catalytic domain is a major determinant for the substrate specificity of the Enpp family enzymes. Furthermore, along with biochemical and biological data, these structures suggest that the produced LPAs are delivered from the active site to cognate G protein-coupled receptors through a hydrophobic channel.

PubMed: 21240269
DOI: 10.1038/nsmb.1998

実験手法

X-RAY DIFFRACTION (1.8 Å)