1JDJ

CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH 2-FLUORO-6-CHLOROPURINE

1JDJ の概要

• エントリーDOI: 10.2210/pdb1jdj/pdb
• 関連するPDBエントリー: 1EVY 1EVZ
• 分子名称: GLYCEROL-3-PHOSPHATE DEHYDROGENASE, 6-CHLORO-2-FLUOROPURINE, PENTADECANE, ... (4 entities in total)
• 機能のキーワード: dehydrogenase, oxidoreductase
• 由来する生物種: Leishmania mexicana
• 細胞内の位置: Glycosome : P90551
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39702.79

構造登録者

Suresh, S.,Wisedchaisri, G.,Kennedy, K.J.,Verlinde, C.L.M.J.,Gelb, M.H.,Hol, W.G.J. (登録日: 2001-06-14, 公開日: 2002-06-14, 最終更新日: 2023-08-16)

主引用文献

Choe, J.,Suresh, S.,Wisedchaisri, G.,Kennedy, K.J.,Gelb, M.H.,Hol, W.G.
Anomalous differences of light elements in determining precise binding modes of ligands to glycerol-3-phosphate dehydrogenase.
Chem.Biol., 9:1189-1197, 2002

PubMed Abstract: Pathogenic protozoa such as Trypanosome and Leishmania species cause tremendous suffering worldwide. Because of their dependence on glycolysis for energy, the glycolytic enzymes of these organisms, including glycerol-3-phosphate dehydrogenase (GPDH), are considered attractive drug targets. Using the adenine part of NAD as a lead compound, several 2,6-disubstituted purines were synthesized as inhibitors of Leishmania mexicana GPDH (LmGPDH). The electron densities for the inhibitor 2-bromo-6-chloro-purine bound to LmGPDH using a "conventional" wavelength around 1 A displayed a quasisymmetric shape. The anomalous signals from data collected at 1.77 A clearly indicated the positions of the halogen atoms and revealed the multiple binding modes of this inhibitor. Intriguing differences in the observed binding modes of the inhibitor between very similarly prepared crystals illustrate the possibility of crystal-to-crystal variations in protein-ligand complex structures.

PubMed: 12445769
DOI: 10.1016/S1074-5521(02)00243-0

実験手法

X-RAY DIFFRACTION (2.2 Å)