AI Article Synopsis
- The study explores how the malaria-causing parasite has evolved mechanisms to infiltrate various host cells using the MyoA motor protein and its associated MTIP.
- The researchers present a crystal structure of Plasmodium MTIP in three conformations, highlighting significant conformational shifts in its C-terminal domain upon interacting with MyoA-tail, which creates binding sites for MyoA's hydrophobic chains.
- The findings suggest that the MyoA helix can inhibit parasite growth, paving the way for potential development of new antimalarial treatments.
Article Abstract
The causative agents of malaria have developed a sophisticated machinery for entering multiple cell types in the human and insect hosts. In this machinery, a critical interaction occurs between the unusual myosin motor MyoA and the MyoA-tail Interacting Protein (MTIP). Here we present one crystal structure that shows three different conformations of Plasmodium MTIP, one of these in complex with the MyoA-tail, which reveal major conformational changes in the C-terminal domain of MTIP upon binding the MyoA-tail helix, thereby creating several hydrophobic pockets in MTIP that are the recipients of key hydrophobic side chains of MyoA. Because we also show that the MyoA helix is able to block parasite growth, this provides avenues for designing antimalarials.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1458759 | PMC |
| http://dx.doi.org/10.1073/pnas.0510907103 | DOI Listing |
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