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

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• 作者：Benjamin G. Bobay ; Am ; a L. Stewart ; Ashley T. Tucker ; Richele J. Thompson ; Kristen M. Varney ; John Cavanagh
• 关键词：Calbindin-D28K ; Caspase-3 ; Isothermal titration calorimetry ; Molecular docking
• 刊名：FEBS Letters
• 出版年：2012
• 出版时间：19 October, 2012
• 年：2012
• 卷：586
• 期：20
• 页码：3582-3589
• 全文大小：1690 K

文摘

The 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 interactions

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