Structure of an insect epsilon class glutathione S-transferase from the malaria vector Anopheles gambiae provides an explanation for the high DDT-detoxifying activity

Journal of Structural Biology

Volumn 164, Issue 2, 2008, Pages 228-235

  Wang, Yujun ^a   Qiu, Li ^a   Ranson, Hilary ^b   Lumjuan, Nongkran ^b   Hemingway, Janet ^b   Setzer, William N ^a   Meehan, Edward J ^a   Chen, Liqing ^a  

^a NASA HEADQUARTERS   (United States)

^b LIVERPOOL SCHOOL OF TROPICAL MEDICINE   (United Kingdom)

Author keywords

agGSTe2; Anopheles gambiae; Crystal structure; DDT resistance; Glutathione S transferase; Malaria

Indexed keywords

1,1 DICHLORO 2,2 BIS(4 CHLOROPHENYL)ETHYLENE; ARGININE; CHLORPHENOTANE; GLUTAMINE; GLUTATHIONE TRANSFERASE; PHENYLALANINE; S HEXYLGLUTATHIONE; GLUTATHIONE; INSECTICIDE; PROTEIN BINDING;

ANOPHELES GAMBIAE; ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CONFORMATION; CRYSTAL STRUCTURE; DISEASE CARRIER; ENZYME BINDING; ENZYME STRUCTURE; HYDROGEN BOND; INSECT; METABOLISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; ANIMAL; CHEMISTRY; DRUG RESISTANCE; ENZYMOLOGY; MALARIA; PROTEIN CONFORMATION; TRANSMISSION; X RAY CRYSTALLOGRAPHY;

ANIMALS; ANOPHELES GAMBIAE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DDT; DRUG RESISTANCE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; INSECT VECTORS; INSECTICIDES; INSECTS; MALARIA; PROTEIN BINDING; PROTEIN CONFORMATION;

ANOPHELES GAMBIAE; HEXAPODA;

EID: 53949123101     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2008.08.003     Document Type: Article

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