Expression, purification, and molecular characterization of plasmodium falciparum FK506-binding protein 35 (PfFKBP35)
The immunosuppressive drug FK506 binds its targets FK506-binding protein (FKBP) family and modulates cellular processes. Recent studies demonstrated that FK506 shows anti-malaria effects. Newly identified FK506-binding protein 35 from Plasmodium falciparum (PfFKBP35) is assumed to be t...
Saved in:
| Main Authors: | , , , , |
|---|---|
| Other Authors: | |
| Format: | Article |
| Language: | English |
| Published: |
2012
|
| Subjects: | |
| Online Access: | https://hdl.handle.net/10356/94928 http://hdl.handle.net/10220/8735 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Institution: | Nanyang Technological University |
| Language: | English |
| Summary: | The immunosuppressive drug FK506 binds its targets FK506-binding protein (FKBP) family and modulates cellular processes.
Recent studies demonstrated that FK506 shows anti-malaria effects. Newly identified FK506-binding protein 35 from Plasmodium falciparum
(PfFKBP35) is assumed to be the molecular target of FK506 in the parasite. Currently, molecular and structural basis of growth
inhibition of the parasite by FK506 remains unclear. In this study, to examine characteristics of PfFKBP35 and also understand its
molecular mechanism of the inhibition by FK506, we have cloned, expressed, and puriWed the full-length PfFKBP35 and its FK506-binding
domain (FKBD). We demonstrate that the full-length PfFKBP35 and the FKBD were properly folded, and suitable for biochemical
and biophysical studies. PfFKBP35 showed a basal activity in inhibiting the phosphatase activity of calcineurin in the absence of FK506,
but the presence of FK506 greatly enhanced its calcineurin-inhibitory activity. Our NMR data indicate that the FKBD binds FK506 with
a high affinity. |
|---|