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

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

Volume: 15 Issue: 10

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

Affiliation:

Keywords: PfHsp70, Hsp40, molecular chaperone, malaria, substrate binding cavity, suppression of MDH aggregation

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.

Cite this article as:

Shonhai Addmore, Botha Melissa, de Beer A. P. Tjaart, Boshoff Aileen and Blatch L. Gregory, Structure-Function Study of a Plasmodium falciparum Hsp70 Using Three Dimensional Modelling and in Vitro Analyses, Protein & Peptide Letters 2008; 15 (10) . https://dx.doi.org/10.2174/092986608786071067