dc.contributor.authorKang, CongBao
dc.contributor.authorYe, Hong
dc.contributor.authorChia, Joel
dc.contributor.authorChoi, Bo-Hwa
dc.contributor.authorDhe-Paganon, Sirano
dc.contributor.authorSimon, Bernd
dc.contributor.authorSchütz, Ulrike
dc.contributor.authorSattler, Michael
dc.contributor.authorYoon, Ho Sup
dc.identifier.citationKang, C., Ye, H., Chia, J., Choi, B.-H., Dhe-Paganon, S., Simon, B., et al. (2013). Functional role of the flexible N-terminal extension of FKBP38 in catalysis. Scientific reports, 3, 1-8.en_US
dc.description.abstractFKBP38 regulates apoptosis through unique interactions with multiple regulators including Bcl-2. Interestingly, the peptidylprolyl isomerase activity of FKBP38 is only detectable when it binds to calcium-saturated calmodulin (CaM/Ca2+). This, in turn, permits the formation of a complex with Bcl-2. FKBP38 thereby provides an important link between isomerase activity and apoptotic pathways. Here, we show that the N-terminal extension (residues 1-32) preceding the catalytic domain of FKBP38 has an autoinhibitory activity. The core isomerase activity of FKBP38 is inhibited by transient interactions involving the flexible N-terminal extension that precedes the catalytic domain. Notably, CaM/Ca2+ binds to this N-terminal extension and thereby releases the autoinhibitory contacts between the N-terminal extension and the catalytic domain, thus potentiating the isomerase activity of FKBP38. Our data demonstrate how CaM/Ca2+ modulates the catalytic activity of FKBP38.en_US
dc.relation.ispartofseriesScientific reportsen_US
dc.rights© 2013 The Authors. This paper was published in Scientific Reports and is made available as an electronic reprint (preprint) with permission of the authors. The paper can be found at the following official DOI: [http://dx.doi.org/10.1038/srep02985]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.en_US
dc.subjectDRNTU::Science::Biological sciences
dc.titleFunctional role of the flexible N-terminal extension of FKBP38 in catalysisen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.description.versionPublished versionen_US

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