1GG5

CRYSTAL STRUCTURE OF A COMPLEX OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AND A CHEMOTHERAPEUTIC DRUG (E09) AT 2.5 A RESOLUTION

1GG5 の概要

• エントリーDOI: 10.2210/pdb1gg5/pdb
• 分子名称: NAD(P)H DEHYDROGENASE [QUINONE] 1, FLAVIN-ADENINE DINUCLEOTIDE, 3-HYDROXYMETHYL-5-AZIRIDINYL-1METHYL-2-[1H-INDOLE-4,7-DIONE]-PROPANOL, ... (4 entities in total)
• 機能のキーワード: flavoprotein, rossmann fold, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P15559
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 127409.10

構造登録者

Faig, M.,Bianchet, M.A.,Winski, S.,Hargreaves, R.,Moody, C.J.,Hudnott, A.R.,Ross, D.,Amzel, L.M. (登録日: 2000-07-12, 公開日: 2001-09-12, 最終更新日: 2023-12-27)

主引用文献

Faig, M.,Bianchet, M.A.,Winski, S.,Hargreaves, R.,Moody, C.J.,Hudnott, A.R.,Ross, D.,Amzel, L.M.
Structure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones.
Structure, 9:659-667, 2001

PubMed Abstract: NAD(P)H:quinone acceptor oxidoreductase (QR1) protects animal cells from the deleterious and carcinogenic effects of quinones and other electrophiles. Remarkably, the same enzyme activates cancer prodrugs that become cytotoxic only after two-electron reduction. QR1's ability to bioactivate quinones and its elevated expression in many human solid tumors makes this protein an excellent target for enzyme-directed drug development. Until now, structural analysis of the mode of binding of chemotherapeutic compounds to QR1 was based on model building using the structures of complexes with simple substrates; no structure of complexes of QR1 with chemotherapeutic prodrugs had been reported.

PubMed: 11587640
DOI: 10.1016/S0969-2126(01)00636-0

実験手法

X-RAY DIFFRACTION (2.5 Å)