Data sets on the interaction of FKBP35 from Plasmodium knowlesi and Hsp90 C-terminal pentapeptide

This dataset provides experimental evidence describing the domain-specific interaction between FK506-binding protein 35 (FKBP35) from Plasmodium knowlesi and the Hsp90 C-terminal pentapeptide motif (MEEVD). The dataset was generated to test the hypothesis that the tetratricopeptide repeat domain (TPRD) of FKBP35 mediates recognition of the Hsp90 MEEVD motif, whereas the catalytic peptidyl-prolyl cis–trans isomerase (PPIase) activity resides within the FK506-binding domain (FKBD).
Recombinant full-length FKBP35 (FL-FKBP35) and three variants—Pk-FKBD, Pk-TPRD, and a calmodulin-binding motif deletion mutant (del-CBM)—were heterologously expressed in Escherichia coli and purified as His-tagged proteins. Protein purity and molecular weights were verified by SDS-PAGE, and the raw gel image is provided in the supplementary dataset. Structural integrity of the recombinant proteins was further evaluated using far-UV circular dichroism spectroscopy.
The dataset includes raw measurements of PPIase catalytic activity, circular dichroism spectra, and surface plasmon resonance (SPR) sensorgrams describing the interaction between FKBP35 proteins and the MEEVD peptide. The catalytic assay data confirm that enzymatic activity is localized within the FKBD domain, while the SPR data demonstrate that detectable MEEVD binding occurs only in constructs containing the TPRD domain. Quantitative binding analysis further indicates comparable dissociation constants for FL-FKBP35 and Pk-TPRD, highlighting the key role of the TPRD region in mediating the FKBP35–Hsp90 interaction.
Collectively, this dataset provides integrated biochemical and biophysical evidence clarifying the structural and functional organization of Pk-FKBP35 and supports future studies investigating FKBP–Hsp90 interactions as potential targets for antimalarial drug discovery.