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在p53-MDM2复合体中的结合诱导折叠.

Hai-Feng Chen¹, Ray Luo

¹Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900, USA.

Journal of the American Chemical Society

|February 17, 2007

概括

此摘要是机器生成的。

p53-MDM2相互作用稳定了MDM2,结合和折叠对功能至关重要. 分子动力学模拟显示了绑定和未绑定MDM2的独特展开路径,突出了结构稳定性的差异.

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科学领域:

分子生物学分子生物学
生物物理学的生物物理.
计算生物学计算生物学

背景情况:

MDM2的N端域与p53的交换激活域结合,降低了转录的调节.
p53结合稳定了MDM2的N端域,表明结合和折叠之间的合.
这种相互依赖对于p53-MDM2复合体内的功能相互作用至关重要.

研究的目的:

为了研究p53-MDM2复合体中结合和折叠的相互依赖.
通过显式溶剂模拟来研究结合和不结合的MDM2 (N) 的分子动力学.

主要方法:

显式溶剂分子动力学 (MD) 模拟.
高温MD模拟用于动力分析.
自由能源景观和过渡状态分析.
用phi值分析预测结构稳定性.

主要成果:

结合和apo-MDM2(N) 通过一个双态过程展开.
绑定的MDM2序列地展开:p53解绑,三级展开,然后二级结构展开.
展开路径不同,与apo-MDM2相比,不稳定的螺旋和三级接触的展开顺序是相反的.
绑定MDM2的过渡状态比apo-MDM2更像本地化和异质化.
稳定螺旋在两种状态中都更像本地螺旋,绑定MDM2中的螺旋II更像本地螺旋.

结论:

这项研究阐明了MDM2与p53结合时与未结合时的不同展开机制.
展开路径和过渡状态的差异强调了p53结合对MDM2结构动态的影响.
研究结果提供了对p53-MDM2相互作用及其调节的分子基础的见解.