5EA2

Crystal Structure of Holo NAD(P)H dehydrogenase, quinone 1

5EA2 の概要

• エントリーDOI: 10.2210/pdb5ea2/pdb
• 関連するPDBエントリー: 5EAI
• 分子名称: NAD(P)H dehydrogenase [quinone] 1, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: nqo1, two-electron reduction of quinone, nad(p)h dehydrogenase, 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: 127425.17

構造登録者

Pidugu, L.S.,Mbimba, J.E.,Ahmad, M.,Pozharski, E.,Sausville, E.A.,Emadi, A.,Toth, E.A. (登録日: 2015-10-15, 公開日: 2016-02-10, 最終更新日: 2023-09-27)

主引用文献

Pidugu, L.S.,Mbimba, J.C.,Ahmad, M.,Pozharski, E.,Sausville, E.A.,Emadi, A.,Toth, E.A.
A direct interaction between NQO1 and a chemotherapeutic dimeric naphthoquinone.
Bmc Struct.Biol., 16:1-1, 2016

PubMed Abstract: Multimeric naphthoquinones are redox-active compounds that exhibit antineoplastic, antiprotozoal, and antiviral activities. Due to their multimodal effect on perturbation of cellular oxidative state, these compounds hold great potential as therapeutic agents against highly proliferative neoplastic cells. In our previous work, we developed a series of novel dimeric naphthoquinones and showed that they were selectively cytotoxic to human acute myeloid leukemia (AML), breast and prostate cancer cell lines. We subsequently identified the oxidoreductase NAD(P)H dehydrogenase, quinone 1 (NQO1) as the major target of dimeric naphthoquinones and proposed a mechanism of action that entailed induction of a futile redox cycling.

PubMed: 26822308
DOI: 10.1186/s12900-016-0052-x

実験手法

X-RAY DIFFRACTION (2.01 Å)