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Protein & Peptide Letters

Author(s): Addmore Shonhai, Melissa Botha, Tjaart A. P. de Beer, Aileen Boshoff and Gregory L. Blatch

DOI: 10.2174/092986608786071067

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Structure-Function Study of a Plasmodium falciparum Hsp70 Using Three Dimensional Modelling and in Vitro Analyses

Page: [1117 - 1125] Pages: 9

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Abstract

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