2ON5
Structure of NaGST-2
Summary for 2ON5
Entry DOI | 10.2210/pdb2on5/pdb |
Related | 1TW9 2ON7 |
Descriptor | Na Glutathione S-transferase 2, 1,2-ETHANEDIOL, GLUTATHIONE, ... (4 entities in total) |
Functional Keywords | gst; hookworm; necator, transferase |
Biological source | Necator americanus |
Total number of polymer chains | 8 |
Total formula weight | 196521.41 |
Authors | Asojo, O.A.,Ngamelue, M.,Homma, H.,Goud, G.,Zhan, B.,Hotez, P.J. (deposition date: 2007-01-23, release date: 2007-08-07, Last modification date: 2023-08-30) |
Primary citation | Asojo, O.A.,Homma, K.,Sedlacek, M.,Ngamelue, M.,Goud, G.N.,Zhan, B.,Deumic, V.,Asojo, O.,Hotez, P.J. X-ray structures of Na-GST-1 and Na-GST-2 two glutathione s-transferase from the human hookworm Necator americanus Bmc Struct.Biol., 7:42-42, 2007 Cited by PubMed Abstract: Human hookworm infection is a major cause of anemia and malnutrition of adults and children in the developing world. As part of on-going efforts to control hookworm infection, The Human Hookworm Vaccine Initiative has identified candidate vaccine antigens from the infective L3 larval stages and adult stages of the parasite. Adult stage antigens include the cytosolic glutathione-S-transferases (GSTs). Nematode GSTs facilitate the inactivation and degradation of a variety of electrophilic substrates (drugs) via the nucleophilic addition of reduced glutathione. Parasite GSTs also play significant roles in multi-drug resistance and the modulation of host-immune defense mechanisms. PubMed: 17594497DOI: 10.1186/1472-6807-7-42 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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