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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Modeling the Relationship between the p53 C-Terminal Domain and Its Binding Partners Using Molecular Dynamics
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Modeling the Relationship between the p53 C-Terminal Domain and Its Binding Partners Using Molecular Dynamics

机译：使用分子动力学模拟p53 C末端结构域与其结合伴侣之间的关系

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摘要

Fifty percent of all cancer cases result from mutations of the TP53 gene, which encodes the tumor suppressor p53, and it is hypothesized that the p53-mediated checkpoint pathway is compromised in most of the remaining cases. The p53 C-terminal domain (CTD) is an important site of p53 regulation but by nature is difficult to study, as it is intrinsically disordered. In this study, we performed molecular dynamics simulations on the p53 CTD and five known regulatory binding partners. We identified distinct trends in fluctuation within and around the p53 CTD binding site on each partner demonstrating a behavior that facilitates association. Further. we present evidence that the size of the hydrophobic pocket in each p53 CTD binding site governs the secondary structure of the p53 CTD when in the bound state. This information will be useful for predicting new binding partners for the p53 CTD. identifying interacting regions within other known partners, and discovering inhibitors that provide additional points of control over p53 activity.
机译：在所有癌症病例中，有百分之五十是由TP53基因的突变引起的，该基因编码肿瘤抑制因子p53，据推测，在其余大多数病例中，p53介导的检查点途径受到损害。 p53 C末端结构域（CTD）是p53调控的重要位点，但由于其固有的无序性，因此很难进行研究。在这项研究中，我们对p53 CTD和五个已知的调节结合配偶体进行了分子动力学模拟。我们在每个伴侣的p53 CTD结合位点之内和周围发现了明显的波动趋势，表明了促进关联的行为。进一步。我们提供的证据表明，在处于结合状态时，每个p53 CTD结合位点中疏水口袋的大小决定着p53 CTD的二级结构。该信息将有助于预测p53 CTD的新结合伴侣。在其他已知伴侣中鉴定相互作用区域，并发现可提供p53活性控制点的抑制剂。

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