Structure-function study of a Plasmodium falciparum Hsp70 using three dimensional modelling and in Vitro analyses

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Shonhai, Addmore, Botha, Melissa, de Beer, Tjaart A. P, Boshoff, Aileen and Blatch, Gregory L (2008) Structure-function study of a Plasmodium falciparum Hsp70 using three dimensional modelling and in Vitro analyses. Protein and Peptide Letters, 15 (10). pp. 1117-1125. ISSN 0929-8665

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 chaperone's substrate binding cavity compromised the protein's chaperone function.

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Additional Information

Online ISSN: 1875-5305

Item type Article
URI https://vuir.vu.edu.au/id/eprint/8146
DOI https://doi.org/10.2174/092986608786071067
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Historical > FOR Classification > 1101 Medical Biochemistry and Metabolomics
Keywords ResPubID22200. PfHsp70, Hsp40, molecular chaperones, malaria, substrate binding cavity, suppression of MDH aggregation, heat shock proteins
Citations in Scopus 45 - View on Scopus
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