6OIU
X-ray crystal structure of the ectodomain of the Toxoplasma gondii ME49 Aminopeptidase N (TGME49_224350)
Summary for 6OIU
| Entry DOI | 10.2210/pdb6oiu/pdb |
| Descriptor | Aminopeptidase N, ZINC ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | aminopeptidase n, m1 aminopeptidase, metallo-exopeptidase, hydrolase |
| Biological source | Toxoplasma gondii (strain ATCC 50611 / Me49) |
| Total number of polymer chains | 4 |
| Total formula weight | 413547.99 |
| Authors | McGowan, S.,Drinkwater, N. (deposition date: 2019-04-09, release date: 2020-09-30, Last modification date: 2023-10-11) |
| Primary citation | Marijanovic, E.M.,Weronika Swiderska, K.,Andersen, J.,Aschenbrenner, J.C.,Webb, C.T.,Drag, M.,Drinkwater, N.,McGowan, S. X-ray crystal structure and specificity of the Toxoplasma gondii ME49 TgAPN2. Biochem.J., 477:3819-3832, 2020 Cited by PubMed Abstract: Toxoplasmosis is a parasitic disease caused by infection with Toxoplasma gondii that currently has few therapeutic options. The M1 aminopeptidase enzymes have been shown to be attractive targets for anti-parasitic agents and/or vaccine candidates, suggesting potential to re-purpose inhibitors between parasite M1 aminopeptidase targets. The M1 aminopeptidase TgAPN2 has been suggested to be a potential new drug target for toxoplasmosis. Here we investigate the structure and function of TgAPN2, a homologue of the antimalarial drug target PfA-M1, and evaluate the capacity to use inhibitors that target PfA-M1 against TgAPN2. The results show that despite a similar overall fold, the TgAPN2 has a unique substrate specificity and inhibition profile. Sequence and structure differences are investigated and show how comparative structure-activity relationships may provide a route to obtaining potent inhibitors of TgAPN2. PubMed: 32926129DOI: 10.1042/BCJ20200569 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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