Structure-Function Study of a Plasmodium falciparum Hsp70 Using Three Dimensional Modelling and in Vitro Analyses
Tjaart A. P. de Beer,
Gregory L. Blatch.
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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