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- W4226182758 endingPage "e1010408" @default.
- W4226182758 startingPage "e1010408" @default.
- W4226182758 abstract "Malaria is responsible for half a million deaths annually and poses a huge economic burden on the developing world. The mosquito-borne parasites (Plasmodium spp.) that cause the disease depend upon an unconventional actomyosin motor for both gliding motility and host cell invasion. The motor system, often referred to as the glideosome complex, remains to be understood in molecular terms and is an attractive target for new drugs that might block the infection pathway. Here, we present the high-resolution structure of the actomyosin motor complex from Plasmodium falciparum. The complex includes the malaria parasite actin filament (PfAct1) complexed with the class XIV myosin motor (PfMyoA) and its two associated light-chains. The high-resolution core structure reveals the PfAct1:PfMyoA interface in atomic detail, while at lower-resolution, we visualize the PfMyoA light-chain binding region, including the essential light chain (PfELC) and the myosin tail interacting protein (PfMTIP). Finally, we report a bare PfAct1 filament structure at improved resolution." @default.
- W4226182758 created "2022-05-05" @default.
- W4226182758 creator A5001343037 @default.
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- W4226182758 date "2022-04-04" @default.
- W4226182758 modified "2023-09-25" @default.
- W4226182758 title "High-resolution structures of malaria parasite actomyosin and actin filaments" @default.
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- W4226182758 doi "https://doi.org/10.1371/journal.ppat.1010408" @default.
- W4226182758 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35377914" @default.
- W4226182758 hasPublicationYear "2022" @default.
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