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

被引：12

作者：

Bobay, Benjamin G. ^{[1
]}

Stewart, Amanda L. ^{[1
]}

Tucker, Ashley T. ^{[1
]}

Thompson, Richele J. ^{[1
]}

Varney, Kristen M. ^{[2
]}

Cavanagh, John ^{[1
]}

机构：

[1] N Carolina State Univ, Dept Mol & Struct Biochem, Raleigh, NC 27695 USA

[2] Univ Maryland, Sch Med, Dept Biochem & Mol Biol, Baltimore, MD 21201 USA

来源：

FEBS LETTERS | 2012年 / 586卷 / 20期

关键词：

Calbindin-D28K; Caspase-3; Isothermal titration calorimetry; Molecular docking; PROTEIN STRUCTURES; CELL-DEATH; APOPTOSIS; BINDING; ACTIVATION; TRANSITIONS; EXPRESSION; NEURONS; CPP32;

D O I：

10.1016/j.febslet.2012.08.032

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：3582 / 3589

页数：8

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