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Title: Expression, purification, and molecular characterization of plasmodium falciparum FK506-binding protein 35 (PfFKBP35)
Authors: Yoon, Hye Rim
Kang, Cong Bao
Chia, Joel
Tang, Kai
Yoon, Ho Sup
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2007
Source: Yoon, H. R., Kang, C. B., Chia, J., Tang, K., & Yoon, H. S. (2007). Expression, purification, and molecular characterization of plasmodium falciparum FK506-binding protein 35 (PfFKBP35). Protein Expression and Purification, 53(1), 179-185.
Series/Report no.: Protein expression and purification
Abstract: 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.
ISSN: 10465928
DOI: 10.1016/j.pep.2006.12.019
Rights: © 2006 Elsevier. This is the author created version of a work that has been peer reviewed and accepted for publication by Protein Expression and Purification, Elsevier. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at:
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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