Endogenous structure of antimalarial target PfATP4 reveals an apicomplexan-specific P-type ATPase modulator.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 41115914.
- Also identified by DOI 10.1038/s41467-025-64815-y and PMC identifier 12537908.
- Licence recorded as CC BY-NC-ND.
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Abstract
The Plasmodium falciparum sodium efflux pump PfATP4 is a leading antimalarial target, but suffers from a lack of high-resolution structural information needed to identify functionally important features in conserved regions and guide rational design of next generation inhibitors. Here, we determine a 3.7 Å cryoEM structure of PfATP4 purified from CRISPR-engineered P. falciparum parasites, revealing a previously unknown, apicomplexan-specific binding partner, PfABP, which forms a conserved, likely modulatory interaction with PfATP4. The discovery of PfABP presents an unexplored avenue for designing PfATP4 inhibitors.
Medical subject headings
- Plasmodium falciparum
- Protozoan Proteins
- Antimalarials
- Adenosine Triphosphatases