NMR assignments of the FK506-binding domain of FK506-binding protein 35 from Plasmodium vivax.
نویسندگان
چکیده
PvFKBP35 is a member of the FK506 binding protein family (FKBP) from Plasmodium vivax. The FK506-binding domain of PvFKBP35 shows a canonical peptidylprolyl cis-trans isomerase (PPIase) activity. To understand the role of PvFKBP35 in the parasite, we have performed NMR studies. Here, we report the assignment of the FK506-binding domain of PvFKBP35.
منابع مشابه
1H, 13C, and 15N resonance assignments of FK506-binding domain of Plasmodium falciparum FKBP35.
The immunosuppressant FK506 binds Plasmodium falciparum FK-506 binding protein 35 (PfFKBP35) and shows anti-malarial activity. To understand molecular mechanism of the drug on the parasite, we have done NMR studies. Here, we report the assignment of FK506-binding domain of PfFKBP35.
متن کاملN resonance assignments of FK506-binding domain of Plasmodium falciparum FKBP35
The immunosuppressant FK506 binds Plasmodium falciparum FK-506 binding protein 35 (PfFKBP35) and shows anti-malarial activity. To understand molecular mechanism of the drug on the parasite, we have done NMR studies. Here, we report the assignment of FK506-binding domain of PfFKBP35.
متن کاملExpression, 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 the molecular target of FK506 in the parasite. Currently, molecular and structural basis of growth inhibition of...
متن کاملTwo crystal structures of the FK506-binding domain of Plasmodium falciparum FKBP35 in complex with rapamycin at high resolution.
Antimalarial chemotherapy continues to be challenging in view of the emergence of drug resistance, especially artemisinin resistance in Southeast Asia. It is critical that novel antimalarial drugs are identified that inhibit new targets with unexplored mechanisms of action. It has been demonstrated that the immunosuppressive drug rapamycin, which is currently in clinical use to prevent organ-tr...
متن کاملOptimized Method for Purification of Expressed Plasmodium Vivax Duffy Binding Protein-II (PvDBP-II): Implication for Vivax Malaria Vaccine Development
Background: The purity and correct folding of a recombinant protein is critical for any structural, biochemical and vaccine design studies. Plasmodium vivax Duffy binding protein-II is a leading vaccine candidate for vivax malaria. In the present study, the purification process of recombinant DBP-IX (a variant form of PvDBP-II) was optimized to achieve the highest yield and purity. Moreover, ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Biomolecular NMR assignments
دوره 3 2 شماره
صفحات -
تاریخ انتشار 2009