The spatial orientation of domains of the heat shock protein 70 from Plasmodium falciparum (PfHsp70) were mapped based on a three-dimensional model of the protein. Purified PfHsp70 displayed chaperone activity in vitro. Amino acid substitutions introduced in the chaperones substrate binding cavity compromised the proteins chaperone function.
Keywords: PfHsp70, Hsp40, molecular chaperone, malaria, substrate binding cavity, suppression of MDH aggregation
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