Structure-function study of a Plasmodium falciparum Hsp70 using three dimensional modelling and in vitro analyses.
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.
Shonhai
Addmore
A
Department of Biochemistry, Microbiology and Biotechnology, Rhodes University, Grahamstown 6140, South Africa. g.blatch@ru.ac.za
Botha
Melissa
M
de Beer
Tjaart A P
TA
Boshoff
Aileen
A
Blatch
Gregory L
GL
D000255:Adenosine Triphosphate / Q000378:metabolism / Q000494:pharmacology; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004305:Dose-Response Relationship, Drug; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008291:Malate Dehydrogenase / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum; D011485:Protein Binding / Q000187:drug effects; D011487:Protein Conformation; D015800:Protozoan Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013696:Temperature
D018840:HSP70 Heat-Shock Proteins; D015800:Protozoan Proteins; D000255:Adenosine Triphosphate; D008291:Malate Dehydrogenase