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

Shonhai, Addmore and Botha, Melissa and de Beer, Tjaart A. P and 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

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

Item Type: Article
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Online ISSN: 1875-5305

Uncontrolled Keywords: ResPubID22200. PfHsp70, Hsp40, molecular chaperones, malaria, substrate binding cavity, suppression of MDH aggregation, heat shock proteins
Subjects: Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
FOR Classification > 1101 Medical Biochemistry and Metabolomics
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Depositing User: VUIR
Date Deposited: 30 Apr 2012 03:51
Last Modified: 28 Jan 2015 04:13
URI: http://vuir.vu.edu.au/id/eprint/8146
DOI: 10.2174/092986608786071067
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Citations in Scopus: 10 - View on Scopus

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