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Among these exported components is a single heat-shock 70\u2005kDa 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 \u03b2-sandwich and \u03b1-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.<\/jats:p>","DOI":"10.1107\/s2053230x2001208x","type":"journal-article","created":{"date-parts":[[2020,9,29]],"date-time":"2020-09-29T10:22:51Z","timestamp":1601374971000},"page":"495-500","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":10,"title":["Structure of the substrate-binding domain of <i>Plasmodium falciparum<\/i> heat-shock protein 70-x"],"prefix":"10.1107","volume":"76","author":[{"given":"Julia","family":"Schmidt","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ioannis","family":"Vakonakis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2020,9,28]]},"reference":[{"key":"ow5024_bb1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/BF00175490","volume":"38","author":"Boorstein","year":"1994","journal-title":"J. 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