Ontology highlight
ABSTRACT:
SUBMITTER: Schmidt J
PROVIDER: S-EPMC7531245 | biostudies-literature | 2020 Oct
REPOSITORIES: biostudies-literature
Schmidt Julia J Vakonakis Ioannis I
Acta crystallographica. Section F, Structural biology communications 20200928 Pt 10
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. ...[more]