ArticleActa crystallographica. Section F, Structural biology communications2015
The X-ray structure of Plasmodium falciparum dihydroorotate dehydrogenase bound to a potent and selective N-phenylbenzamide inhibitor reveals novel binding-site interactions.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 23 citations in OpenAlex.
- Design of Anti-infectious Agents from Lawsone in a Three-Component Reaction with Aldehydes and Isocyanides.ACS omega · 2022Article
- Antimalarial Inhibitors Targeting Epigenetics or Mitochondria inMolecules (Basel, Switzerland) · 2021Review
- Synthesis and Antiplasmodial Activity of 1,2,3-Triazole-Naphthoquinone Conjugates.Molecules (Basel, Switzerland) · 2019Article
- Insights into Integrated Lead Generation and Target Identification in Malaria and Tuberculosis Drug Discovery.Accounts of chemical research · 2017Article
- Crystal structure of truncated aspartate transcarbamoylase from Plasmodium falciparum.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Identification of New Human Malaria Parasite Plasmodium falciparum Dihydroorotate Dehydrogenase Inhibitors by Pharmacophore and Structure-Based Virtual Screening.Journal of chemical information and modeling · 2016Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Plasmodium species are protozoan parasites that are the causative agent of malaria. Malaria is a devastating disease, and its treatment and control have been hampered by the propensity of the parasite to become drug-resistant. Dihydroorotate dehydrogenase (DHODH) has been identified as a promising new target for the development of antimalarial agents. Here, the X-ray structure of P. falciparum DHODH bound to a potent and selective N-phenylbenzamide-based inhibitor (DSM59) is described at 2.3 Å resolution. The structure elucidates novel binding-site interactions and shows how conformational flexibility of the enzyme leads to the ability to bind diverse chemical structures with high affinity. This information provides new insight into the design of high-affinity DHODH inhibitors for the treatment of malaria.
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