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...

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Main Authors:	Yoon, Hye Rim, Kang, Cong Bao, Chia, Joel, Tang, Kai, Yoon, Ho Sup
Other Authors:	School of Biological Sciences
Format:	Article
Language:	English
Published:	2012
Subjects:	DRNTU::Science::Biological sciences
Online Access:	https://hdl.handle.net/10356/94928 http://hdl.handle.net/10220/8735
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Institution:	Nanyang Technological University
Language:	English

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spelling	sg-ntu-dr.10356-949282023-02-28T17:03:39Z Expression, purification, and molecular characterization of plasmodium falciparum FK506-binding protein 35 (PfFKBP35) Yoon, Hye Rim Kang, Cong Bao Chia, Joel Tang, Kai Yoon, Ho Sup School of Biological Sciences DRNTU::Science::Biological sciences 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. Accepted version 2012-10-09T06:00:19Z 2019-12-06T19:04:52Z 2012-10-09T06:00:19Z 2019-12-06T19:04:52Z 2007 2007 Journal Article 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. 10465928 https://hdl.handle.net/10356/94928 http://hdl.handle.net/10220/8735 10.1016/j.pep.2006.12.019 en Protein expression and purification © 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: http://dx.doi.org/10.1016/j.pep.2006.12.019. application/pdf
institution	Nanyang Technological University
building	NTU Library
continent	Asia
country	Singapore Singapore
content_provider	NTU Library
collection	DR-NTU
language	English
topic	DRNTU::Science::Biological sciences
spellingShingle	DRNTU::Science::Biological sciences Yoon, Hye Rim Kang, Cong Bao Chia, Joel Tang, Kai Yoon, Ho Sup Expression, purification, and molecular characterization of plasmodium falciparum FK506-binding protein 35 (PfFKBP35)
description	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.
author2	School of Biological Sciences
author_facet	School of Biological Sciences Yoon, Hye Rim Kang, Cong Bao Chia, Joel Tang, Kai Yoon, Ho Sup
format	Article
author	Yoon, Hye Rim Kang, Cong Bao Chia, Joel Tang, Kai Yoon, Ho Sup
author_sort	Yoon, Hye Rim
title	Expression, purification, and molecular characterization of plasmodium falciparum FK506-binding protein 35 (PfFKBP35)
title_short	Expression, purification, and molecular characterization of plasmodium falciparum FK506-binding protein 35 (PfFKBP35)
title_full	Expression, purification, and molecular characterization of plasmodium falciparum FK506-binding protein 35 (PfFKBP35)
title_fullStr	Expression, purification, and molecular characterization of plasmodium falciparum FK506-binding protein 35 (PfFKBP35)
title_full_unstemmed	Expression, purification, and molecular characterization of plasmodium falciparum FK506-binding protein 35 (PfFKBP35)
title_sort	expression, purification, and molecular characterization of plasmodium falciparum fk506-binding protein 35 (pffkbp35)
publishDate	2012
url	https://hdl.handle.net/10356/94928 http://hdl.handle.net/10220/8735
_version_	1759856946188386304

Expression, purification, and molecular characterization of plasmodium falciparum FK506-binding protein 35 (PfFKBP35)

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