Biophysical analysis of Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop) reveals a monomer that is characterised by folded segments connected by flexible linkers.
Plasmodium falciparum causes the most lethal form of malaria. The cooperation of heat shock protein (Hsp) 70 and 90 is thought to facilitate folding of select group of cellular proteins that are crucial for cyto-protection and development of the parasites. Hsp70 and Hsp90 are brought into a function...
Main Authors: | Stanley Makumire, Tawanda Zininga, Juha Vahokoski, Inari Kursula, Addmore Shonhai |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2020-01-01
|
Series: | PLoS ONE |
Online Access: | https://doi.org/10.1371/journal.pone.0226657 |
Similar Items
-
Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a Nucleotide-Dependent Fashion and Exhibits Ligand Selectivity.
by: Tawanda Zininga, et al.
Published: (2015-01-01) -
The Link That Binds: The Linker of Hsp70 as a Helm of the Protein’s Function
by: Graham Chakafana, et al.
Published: (2019-09-01) -
Inhibition of Plasmodium falciparum Hsp70-Hop partnership by 2-phenylthynesulfonamide
by: Tshifhiwa Muthelo, et al.
Published: (2022-09-01) -
Overexpression, Purification and Characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) Protein.
by: Tawanda Zininga, et al.
Published: (2015-01-01) -
Supporting data on characterisation of linker switch mutants of Plasmodium falciparum heat shock protein 110 and canonical Hsp70
by: Graham Chakafana, et al.
Published: (2021-08-01)