- Title
- Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion
- Creator
- Ziningwa, Tawanda, Achilonu, Ikechukwu, Hoppe, Heinrich C, Prinsloo, Earl, Dirr, Heinrich W, Shonhai, Addmore
- Subject
- To be catalogued
- Date
- 2016
- Type
- text
- Type
- article
- Identifier
- http://hdl.handle.net/10962/431765
- Identifier
- vital:72802
- Identifier
- xlink:href="https://doi.org/10.1007/s12192-016-0678-4"
- Description
- The role of molecular chaperones, among them heat shock proteins (Hsps), in the development of malaria parasites has been well documented. Hsp70s are molecular chaperones that facilitate protein folding. Hsp70 proteins are composed of an N-terminal nucleotide binding domain (NBD), which confers them with ATPase activity and a Cterminal substrate binding domain (SBD). In the ADPbound state, Hsp70 possesses high affinity for substrate and releases the folded substrate when it is bound to ATP. The two domains are connected by a conserved linker segment. Hsp110 proteins possess an extended lid segment, a feature that distinguishes them from canonical Hsp70s.
- Format
- computer, online resource, application/pdf, 1 online resource (15 pages), pdf
- Publisher
- SpringerLink
- Language
- English
- Relation
- Cell Stress and Chaperones, Zininga, T., Achilonu, I., Hoppe, H., Prinsloo, E., Dirr, H.W. and Shonhai, A., 2016. Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion. Cell Stress and Chaperones, 21, pp.499-513, Cell Stress and Chaperones volume 21 p. 499 2016 1466-1268
- Rights
- Publisher
- Rights
- Use of this resource is governed by the terms and conditions of the SpringerLink Terms of Use Statement ( https://link.springer.com/termsandconditions)
- Rights
- Open Access
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Collections
Prinsloo, Earl (Dr)
RU DST/NRF SARChI for Biotechnology Innovation and Engagement
Hoppe, Heinrich C (Prof)
RU Department of Chemistry
RU Department of Biochemistry, Microbiology and Bioinformatics
SDG 03. Good Health and Well-Being
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