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

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

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Title: Expression, purification, and molecular characterization of plasmodium falciparum FK506-binding protein 35 (PfFKBP35)
Author: Yoon, Hye Rim; Kang, Cong Bao; Chia, Joel; Tang, Kai; Yoon, Ho Sup
Copyright year: 2007
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.
Subject: DRNTU::Science::Biological sciences.
Type: Journal Article
Series/ Journal Title: Protein expression and purification
School: School of Biological Sciences
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: http://dx.doi.org/10.1016/j.pep.2006.12.019.
Version: Accepted version

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