What is it about?

Malaria is endemeic in about 100 countries in the world and resistances of Plasmodium parasites to existing treatments is an issue. The paarsite subtilisin-like protease 1 plays an essentail role for the parasite to egress from human hepatic and erytthrocytic cells and emerged as an interesting drug-target to design new generation of anti-malarial candidates. In this issue, we describe the first 3D-structure of Sub1 in complex with a specific inhibitor.

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Why is it important?

Informations provided by these structural data will help cehemists to design and synthetise optimized Sub1 inhibitor that could eventually become new lead compounds to figth malaria.

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This page is a summary of: 3D structures of the Plasmodium vivax subtilisin-like drug target SUB1 reveal conformational changes to accommodate a substrate-derived α-ketoamide inhibitor, Acta Crystallographica Section D Structural Biology, July 2023, International Union of Crystallography,
DOI: 10.1107/s2059798323004710.
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