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ResearchBIORXIVThursday, March 26, 2026 · March 26, 2026

Preprint: Discovery of Plasmodium falciparum SR12 as a GOLD-Domain seven transmembrane protein regulating GPCR trafficking in mammalian cells

WHY IT MATTERS

This research could lead to new antimalarial drugs that work differently than current ones, which is critical because malaria parasites are increasingly resistant to existing treatments and malaria still kills hundreds of thousands of people annually.

Scientists discovered a new protein called SR12 in the malaria parasite that works similarly to proteins in human cells. This protein might be a good target for creating new malaria drugs, especially since the parasite is becoming resistant to current treatments. The researchers used computer modeling to understand how this protein is structured and how it functions.

Discovery of Plasmodium falciparum SR12 as a GOLD-Domain seven transmembrane protein regulating GPCR trafficking in mammalian cells Authors: Pereira, P. H. S. et al. Server: bioRxiv Category: cell biology Abstract: Considered a significant public health issue, the growing resistance to conventional antimalarials necessitates the identification of new targets for drug development. Given that G protein-coupled receptors (GPCRs) are readily druggable targets, we explored the cellular role and potential structure of a GPCR-like protein identified in the P. falciparum genome, serpentine receptor 12 (SR12). Alphafold structure analysis, coupled with molecular dynamics simulations of SR12, revealed structural similarities to the Golgi dynamics domain (GOLD)-seven-transmembrane helix protein family (GOST protein

Read the original at biorxiv
malariadrug-resistanceantimalarialprotein-structuredrug-development

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