5EA2

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

Summary for 5EA2

• Entry DOI: 10.2210/pdb5ea2/pdb
• Related: 5EAI
• Descriptor: NAD(P)H dehydrogenase [quinone] 1, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: nqo1, two-electron reduction of quinone, nad(p)h dehydrogenase, oxidoreductase
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: P15559
• Total number of polymer chains: 4
• Total formula weight: 127425.17

Authors

Pidugu, L.S.,Mbimba, J.E.,Ahmad, M.,Pozharski, E.,Sausville, E.A.,Emadi, A.,Toth, E.A. (deposition date: 2015-10-15, release date: 2016-02-10, Last modification date: 2023-09-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.01 Å)