3EE2

Structure of human prostaglandin D-synthase (hGSTS1-1) in complex with nocodazole

3EE2 の概要

• エントリーDOI: 10.2210/pdb3ee2/pdb
• 関連するPDBエントリー: 1IYH 1IYI 1PD2 1V40 2CVD
• 分子名称: Glutathione-requiring prostaglandin D synthase, GLUTATHIONE, nocodazole, ... (5 entities in total)
• 機能のキーワード: h-pgds, prostanoid production, inflamation, nocodazole, glutathione transferase sigma, fatty acid biosynthesis, isomerase, lipid synthesis, prostaglandin biosynthesis
• 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: 2
• 化学式量合計: 47402.66

構造登録者

Oakley, A.J. (登録日: 2008-09-04, 公開日: 2008-09-16, 最終更新日: 2023-11-01)

主引用文献

Weber, J.E.,Oakley, A.J.,Christ, A.N.,Clark, A.G.,Hayes, J.D.,Hall, R.,Hume, D.A.,Board, P.G.,Smythe, M.L.,Flanagan, J.U.
Identification and characterisation of new inhibitors for the human hematopoietic prostaglandin D(2) synthase
Eur.J.Med.Chem., 45:447-454, 2010

PubMed Abstract: Prostaglandin D(2) synthesised by the hematopoietic prostaglandin D(2) synthase has a pro-inflammatory effect in allergic asthma, regulating many hallmark characteristics of the disease. Here we describe identification of hematopoietic prostaglandin D(2) synthase inhibitors including cibacron blue, bromosulfophthalein and ethacrynic acid. Expansion around the drug-like ethacrynic acid identified a novel inhibitor, nocodazole, and a fragment representing its aromatic core. Nocodazole binding was further characterised by docking calculations in combination with conformational strain analysis. The benzyl thiophene core was predicted to be buried in the active site, binding in the putative prostaglandin binding site, and a likely hydrogen bond donor site identified. X-ray crystallographic studies supported the predicted binding mode.

PubMed: 19939518
DOI: 10.1016/j.ejmech.2009.10.025

実験手法

X-RAY DIFFRACTION (1.91 Å)