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Structural insights into the calcium-dependent interaction between calbindin-D28K and caspase-3

By Benjamin G. Bobay, Amanda L. Stewart, Ashley T. Tucker, Richele J. Thompson, Kristen M. Varney and John Cavanagh

Abstract

AbstractThe regulation of apoptosis involves a complicated cascade requiring numerous protein interactions including the pro-apoptotic executioner protein caspase-3 and the anti-apoptotic calcium-binding protein calbindin-D28K. Using isothermal titration calorimetry, we show that calbindin-D28K binds caspase-3 in a Ca2+-dependent fashion. Molecular docking and conformational sampling studies of the Ca2+-loaded capase-3/calbindin-D28K interaction were performed in order to isolate potentially crucial intermolecular contacts. Residues in the active site loops of caspase-3 and EF-hands 1 and 2 of calbindin-D28K were shown to be critical to the interaction. Based on these studies, a model is proposed to help understand how calbindin-D28K may deactivate caspase-3 upon binding.Structured summary of protein interactionsCalbindin-D28K and Caspase-3 bind by isothermal titration calorimetry (View interaction

Publisher: Federation of European Biochemical Societies. Published by Elsevier B.V.
Year: 2012
DOI identifier: 10.1016/j.febslet.2012.08.032
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