Structure-Function Study of a Plasmodium falciparum Hsp70 Using Three Dimensional Modelling and in Vitro Analyses
Addmore Shonhai, Melissa Botha, Tjaart A. P. de Beer, Aileen Boshoff and Gregory L. Blatch
Affiliation: Department of Biochemistry, Microbiology and Biotechnology, Rhodes University, Grahamstown 6140, South Africa.
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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