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 
ORCID: 0000-0003-0778-8577
(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 | 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 | 47 - View on Scopus |
| Download/View statistics | View download statistics for this item |
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