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; Gregory   L.   Blatch

doi:10.2174/092986608786071067

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

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Protein & Peptide Letters

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

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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.

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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