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Kang, C.B.* ; Ye, H.* ; Chia, J.* ; Choi, B.H.* ; Dhe-Paganon, S.* ; Simon, B.* ; Schütz, U. ; Sattler, M. ; Yoon, H.S.*

Functional role of the flexible N-terminal extension of FKBP38 in catalysis.

Sci. Rep. 3:2985 (2013)
Verlagsversion Volltext DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
FKBP38 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.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter N-15 Nmr Relaxation ; Steroid-receptor Complexes ; Fk506-binding Protein ; Fk-506 Binding-protein-38 ; Inhibits Apoptosis ; Backbone Dynamics ; Bcl-2 ; Domain ; Immunophilin ; Spectroscopy
ISSN (print) / ISBN 2045-2322
e-ISSN 2045-2322
Zeitschrift Scientific Reports
Quellenangaben Band: 3, Heft: , Seiten: , Artikelnummer: 2985 Supplement: ,
Verlag Nature Publishing Group
Verlagsort London
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)