書誌事項
- タイトル別名
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- Mechanism of Metal Activation of Human Hematopoietic Prostaglandin D Synthase
- サイキン ノ ケンキュウ カラ ヒト ユライ プロスタグランジン D ゴウセイ コウソ ノ キンゾク イオン コウカ ノ メカニズム
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We report the crystal structures of human hematopoietic prostaglandin (PG) D synthase bound to glutathione (GSH) and Ca2+ or Mg2+. Using GSH as a cofactor, prostaglandin D synthase catalyzes the isomerization of PGH2 to PGD2, a mediator for allergy response. The enzyme is a homodimer, and Ca2+ or Mg2+ increases its activity to - 150 % of the basal level, with half maximum effective concentrations of 400 μM for Ca2+ and 50 μM for Mg2+. In the Mg2+-bound form, the ion is octahedrally coordinated by six water molecules at the dimer interface. The water molecules are surrounded by pairs of Asp93, Asp96 and Asp97 from each subunit. Ca2+ is coordinated by five water molecules and an Asp96 from one subunit. The Asp96 residue in the Ca2+-bound form makes hydrogen bonds with two guanidium nitrogen atoms of Arg 14 in the GSH-binding pocket. Mg2+ alters the coordinating water structure and reduces one hydrogen bond between Asp96 and Arg14, thereby changing the interaction between Arg 14 and GSH. This effect explains a four-fold reduction in the Km of the enzyme for GSH. The structure provides insights into how Ca2+ or Mg2+ binding activates human hematopoietic PGD Synthase.
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 45 (Supplement), 16-16, 2003
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
- 1390001204090461184
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- NII論文ID
- 10012663277
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- NII書誌ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL書誌ID
- 6634789
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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
- Crossref
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- 使用不可