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首页> 外文会议>2016 International Conference on Microelectronics, Computing and Communications >Bio-molecular optimized interactions and conformational switches in human ERβ and SRC-1 protein: An in silico approach to suppress tumor in breast cancer malignancies: Computational insight for suppression of tumorigenesis in breast malignancies
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Bio-molecular optimized interactions and conformational switches in human ERβ and SRC-1 protein: An in silico approach to suppress tumor in breast cancer malignancies: Computational insight for suppression of tumorigenesis in breast malignancies

机译：人类ERβ和SRC-1蛋白中生物分子的优化相互作用和构象转换：抑制乳腺癌恶性肿瘤的计算机方法：抑制乳腺癌恶性肿瘤发生的计算机洞察

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A vital female hormone; estrogen activates the β-subunit of estrogen receptor protein (ERβ), which further aids in the suppression of the breast tumor cells with the aid of human SRC-1 (steroid receptor coactivator-1) protein. Though wet laboratory documentation has been documented on this regard but the molecular level studies via optimization operations remains yet unexplored. So, for the purpose, experimentally validated 3D functional structures of the two essential human proteins; ERβ and SRC-1 were extracted, demonstrated and analyzed. Protein-protein docking further led to the complex formation, which was further subjected to optimization and molecular dynamics simulation techniques. Residual contribution from the pre optimized and post optimized simulated protein-protein complex was compared and examined individually, with an additional focus on the binding patterns. The increase in the predominant ionic interactions and side chain-side chain interactions displays the optimized and simulated complex to be greatly interactive one. Mainly, polar negatively charged; Asp87 from ERβ and His1, His5 and Lys2 from SRC-1 played a pivotal role in the protein interaction mechanism after optimization followed by simulation. Statistically significant evaluations from free energy of folding, net area available for solvent accessibility, electrostatic surface potential as well as conformational transition from coils to helices in either of the two proteins additionally affirms the structures to gain stability and strength after optimization and simulation. Therefore, this present study provides a scope to view the residual interactive mode and the most stable interactive protein structures responsible for hindering the tumor proliferation in human breast cancers. For future, it further instigates the biomedical and pharmaceutical field for breast cancer malignancies.
机译：至关重要的女性荷尔蒙；雌激素激活雌激素受体蛋白（ERβ）的β亚基，借助人类SRC-1（类固醇受体共激活因子1）蛋白进一步帮助抑制乳腺肿瘤细胞。尽管在这方面已记录了湿式实验室文件，但通过优化操作进行的分子水平研究仍未探索。因此，为此目的，实验验证了两种基本人类蛋白质的3D功能结构；提取，证明和分析ERβ和SRC-1。蛋白质-蛋白质对接进一步导致了复合物的形成，并对其进行了优化和分子动力学模拟技术。比较并分别检查了前优化和后优化的模拟蛋白质-蛋白质复合物的残留贡献，并特别关注了结合模式。主要的离子相互作用和侧链-侧链相互作用的增加表明优化和模拟的配合物是高度相互作用的。主要是极性带负电荷的；优化并随后进行模拟后，来自ERβ和His1的Asp87，来自SRC-1的His5和Lys2在蛋白质相互作用机制中起着关键作用。从折叠自由能，可用于溶剂可及的净面积，静电表面电势以及两种蛋白质中任一蛋白质从线圈到螺旋的构象转变的统计学意义上的评估都进一步肯定了结构在优化和模拟后可获得稳定性和强度。因此，本研究为观察残留的相互作用模式和最稳定的相互作用蛋白结构提供了一个范围，这些相互作用结构和结构阻碍了人类乳腺癌中肿瘤的扩散。将来，它进一步促进了乳腺癌恶性肿瘤的生物医学和药学领域。

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