書誌事項
- タイトル別名
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- Crystal Structure of Autotaxin, a Lysophospholipase D that Produces Lipid Mediator Lysophosphatidic Acids
- シシツ メディエーター サンセイ コウソ ATX ノ ケッショウ コウゾウ
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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. We solved the crystal structures of mouse ATX alone and in complex with LPAs with different acyl-chain lengths and saturations. The structures reveal a multidomain architecture that may maintain the structure of the hydrophobic pocket, in which the respective LPA molecules are accommodated in distinct conformations. Moreover, our data suggest that the produced LPAs are transferred from the catalytic pocket to cognate receptors through a hydrophobic channel.
収録刊行物
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- 日本結晶学会誌
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日本結晶学会誌 53 (3), 207-212, 2011
日本結晶学会
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詳細情報 詳細情報について
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- CRID
- 1390001204090095360
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- NII論文ID
- 10029371554
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- NII書誌ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL書誌ID
- 11173432
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
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- CiNii Articles
- KAKEN
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- 抄録ライセンスフラグ
- 使用不可