5FWQ

Apo structure of human Leukotriene A4 hydrolase

5FWQ の概要

• エントリーDOI: 10.2210/pdb5fwq/pdb
• 分子名称: HUMAN LEUKOTRIENE A4 HYDROLASE, ACETATE ION, ZINC ION, ... (6 entities in total)
• 機能のキーワード: hydrolase, leukotriene (lt) a4 hydrolase/aminopeptidase, lta4h
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 73186.66

構造登録者

Wittmann, S.K.,Kalinowsky, L.,Kramer, J.,Bloecher, R.,Steinhilber, D.,Pogoryelov, D.,Proschak, E.,Heering, J. (登録日: 2016-02-19, 公開日: 2016-10-05, 最終更新日: 2024-01-10)

主引用文献

Wittmann, S.K.,Kalinowsky, L.,Kramer, J.S.,Bloecher, R.,Knapp, S.,Steinhilber, D.,Pogoryelov, D.,Proschak, E.,Heering, J.
Thermodynamic properties of leukotriene A4hydrolase inhibitors.
Bioorg.Med.Chem., 24:5243-5248, 2016

PubMed Abstract: The leukotriene A hydrolase (LTAH) is a bifunctional enzyme, containing a peptidase and a hydrolase activity both activities having opposing functions regulating inflammatory response. The hydrolase activity is responsible for the conversion of leukotriene A to pro-inflammatory leukotriene B, and hence, selective inhibitors of the hydrolase activity are of high pharmacological interest. Here we present the thermodynamic characterization of structurally distinct inhibitors of the LTAH that occupy different regions of the binding site using different biophysical methods. An in silico method for the determination of stabilized water molecules in the binding site of the apo structure of LTAH is used to interpret the measured thermodynamic data and provided insights for design of novel LTAH inhibitors.

PubMed: 27651294
DOI: 10.1016/j.bmc.2016.08.047

実験手法

X-RAY DIFFRACTION (2.047 Å)