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Publication Abstract from PubMed

The malaria parasite Plasmodium falciparum extensively modifies erythrocytes that it invades by exporting a large complement of proteins to the host cell. Among these exported components is a single heat-shock 70 kDa class protein, PfHsp70-x, that supports the virulence and growth rate of the parasite during febrile episodes. The ATP-binding domain of PfHsp70-x has previously been resolved and showed the presence of potentially druggable epitopes that differ from those on human Hsp70 chaperones. Here, the crystallographic structure of the substrate-binding domain (SBD) of PfHsp70-x is presented in complex with a hydrophobic peptide. The PfHsp70-x SBD is shown to be highly similar to the counterpart from a human erythrocytic Hsp70 chaperone. The binding of substrate at the interface between beta-sandwich and alpha-helical subdomains of this chaperone segment is also conserved between the malaria parasite and humans. It is hypothesized that the parasite may partly exploit human chaperones for intra-erythrocytic trafficking and maintenance of its exported proteome.

Structure of the substrate-binding domain of Plasmodium falciparum heat-shock protein 70-x.,Schmidt J, Vakonakis I Acta Crystallogr F Struct Biol Commun. 2020 Oct 1;76(Pt 10):495-500. doi: , 10.1107/S2053230X2001208X. Epub 2020 Sep 28. PMID:33006578^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.