{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T08:15:18Z","timestamp":1740125718719,"version":"3.37.3"},"reference-count":51,"publisher":"Portland Press Ltd.","issue":"19","license":[{"start":{"date-parts":[[2020,9,14]],"date-time":"2020-09-14T00:00:00Z","timestamp":1600041600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2020,10,16]]},"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.1042\/bcj20200569","type":"journal-article","created":{"date-parts":[[2020,9,14]],"date-time":"2020-09-14T11:08:45Z","timestamp":1600081725000},"page":"3819-3832","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["X-ray crystal structure and specificity of the <i>Toxoplasma gondii<\/i> ME49 <i>Tg<\/i>APN2"],"prefix":"10.1042","volume":"477","author":[{"given":"Emilia M.","family":"Marijanovic","sequence":"first","affiliation":[{"name":"Biomedicine Discovery Institute, Department of Microbiology, Monash University Clayton, Melbourne, VIC 3800, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Karolina","family":"Weronika Swiderska","sequence":"additional","affiliation":[{"name":"Department of Chemical Biology and Bioimaging, Wroclaw University of Science and Technology, Wyb. Wyspianskiego 27, 50-370 Wroclaw, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"James","family":"Andersen","sequence":"additional","affiliation":[{"name":"Biomedicine Discovery Institute, Department of Microbiology, Monash University Clayton, Melbourne, VIC 3800, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jasmin C.","family":"Aschenbrenner","sequence":"additional","affiliation":[{"name":"Biomedicine Discovery Institute, Department of Microbiology, Monash University Clayton, Melbourne, VIC 3800, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chaille T.","family":"Webb","sequence":"additional","affiliation":[{"name":"Biomedicine Discovery Institute, Department of Microbiology, Monash University Clayton, Melbourne, VIC 3800, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marcin","family":"Drag","sequence":"additional","affiliation":[{"name":"Department of Chemical Biology and Bioimaging, Wroclaw University of Science and Technology, Wyb. 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