4EDZ

Crystal structure of hH-PGDS with water displacing inhibitor

4EDZ の概要

• エントリーDOI: 10.2210/pdb4edz/pdb
• 関連するPDBエントリー: 4EDY 4EE0
• 分子名称: Hematopoietic prostaglandin D synthase, GLUTATHIONE, 4-(3-methylisoquinolin-1-yl)-N-[2-(morpholin-4-yl)ethyl]benzamide, ... (5 entities in total)
• 機能のキーワード: inhibitor, solvent replacement, isomerase-isomerase inhibitor complex, isomerase/isomerase inhibitor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: O60760
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 96022.61

構造登録者

Day, J.E.,Thorarensen, A.,Trujillo, J.I. (登録日: 2012-03-27, 公開日: 2012-05-16, 最終更新日: 2024-02-28)

主引用文献

Trujillo, J.I.,Kiefer, J.R.,Huang, W.,Day, J.E.,Moon, J.,Jerome, G.M.,Bono, C.P.,Kornmeier, C.M.,Williams, M.L.,Kuhn, C.,Rennie, G.R.,Wynn, T.A.,Carron, C.P.,Thorarensen, A.
Investigation of the binding pocket of human hematopoietic prostaglandin (PG) D2 synthase (hH-PGDS): a tale of two waters.
Bioorg.Med.Chem.Lett., 22:3795-3799, 2012

PubMed Abstract: The inhibition of hH-PGDS has been proposed as a potential target for the development of anti-allergic and anti-inflammatory drugs. Herein we describe our investigation of the binding pocket of this important enzyme and our observation that two water molecules bind to our inhibitors and the enzyme. A series of compounds were prepared to the probe the importance of the water molecules in determining the binding affinity of the inhibitors to the enzyme. The study provides insight into the binding requirements for the design of potent hH-PGDS inhibitors.

PubMed: 22546671
DOI: 10.1016/j.bmcl.2012.04.004

実験手法

X-RAY DIFFRACTION (2 Å)