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Literature summary for 1.10.5.1 extracted from

  • Leung, K.K.; Shilton, B.H.
    Chloroquine binding reveals flavin redox switch function of quinone reductase 2 (2013), J. Biol. Chem., 288, 11242-11251.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
purified NQO2 in complex with primaquine and chloroquine, hanging drop vapor diffusion method, against reservoirs containing 0.1 M HEPES, pH 7.5, and 1.3-2.0 M (NH4)2SO4, crystals of NQO2-CQ are soaked in 0.001 ml of reducing-soak solution consisting of 0.1 M HEPES, pH 7.5, 2.0 M (NH4)2SO4, 10 mM 1-(3-sulfonatopropyl)-3-carbamoyl-1,4-dihydropyrimidine and 1 mM chloroquine, X-ray diffraction structure determination and analysis at 1.2-1.4 A resolution Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Chloroquine binds preferentially to reduced NQO2, binding mode, closure of a flexible loop (Phe126-Leu136) over the active site, overview Homo sapiens
primaquine binding mode, overview Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P16083
-
-

Synonyms

Synonyms Comment Organism
NQO2
-
Homo sapiens
quinone reductase 2
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD flavin redox switch, structural changes, overview Homo sapiens

General Information

General Information Comment Organism
physiological function quinone reductase 2 is an FAD-linked enzyme and the only known human target of two antimalarial drugs, primaquine and chloroquine, a functional role for NQO2 as a flavin redox switch Homo sapiens