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

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

Journal Name: Protein & Peptide Letters

Volume 15 , Issue 10 , 2008

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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 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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Article Details

VOLUME: 15
ISSUE: 10
Year: 2008
Page: [1117 - 1125]
Pages: 9
DOI: 10.2174/092986608786071067
Price: $58

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