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Protein & Peptide Letters
ISSN (Print): 0929-8665
ISSN (Online): 1875-5305
VOLUME: 15
ISSUE: 10
DOI: 10.2174/092986608786071067      Price:  $58









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

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Author(s): Addmore Shonhai, Melissa Botha, Tjaart A. P. de Beer, Aileen Boshoff and Gregory L. Blatch
Pages 1117-1125 (9)
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
Affiliation:
Department of Biochemistry, Microbiology and Biotechnology, Rhodes University, Grahamstown 6140, South Africa.