Tumor-Suppressor p53TAD1-60 Forms a Fuzzy Complex with Metastasis-Associated S100A4: Structural Insights and Dynamics by an NMR/MD Approach.,ChemBioChem

当前位置： X-MOL 学术 › ChemBioChem › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

Tumor-Suppressor p53TAD1-60 Forms a Fuzzy Complex with Metastasis-Associated S100A4: Structural Insights and Dynamics by an NMR/MD Approach.
ChemBioChem ( IF 2.6 ) Pub Date : 2020-06-08 , DOI: 10.1002/cbic.202000348
Erika F Dudás ₁ , Gyula Pálfy ₁ , Dóra K Menyhárd _{1,

2} , Fanni Sebák _{1,

3} , Péter Ecsédi ₄ , László Nyitray ₄ , Andrea Bodor ₁

Affiliation

Fuzzy in focus: The presented hybrid NMR/MD approach indicates the disorder‐to‐order transition of p53TAD^1–60 upon interaction with S100A4. p53TAD^1–60 remains highly flexible, forms a clamp‐like “fuzzy” complex with three helical regions, and residues L26, M40, W53 are anchored to S100A4.

中文翻译：

肿瘤抑制因子 p53TAD1-60 与转移相关的 S100A4 形成模糊复合物：通过 NMR/MD 方法获得结构见解和动力学。

焦点模糊：所提出的混合 NMR/MD 方法表明 p53TAD ^1-60在与 S100A4 相互作用时发生无序到有序的转变。p53TAD ^1-60保持高度灵活性，形成具有三个螺旋区域的钳状“模糊”复合物，并且残基 L26、M40、W53 锚定到 S100A4。

更新日期：2020-06-08

点击分享查看原文

点击收藏

公开下载

阅读更多本刊最新论文本刊介绍/投稿指南11