Ding Fei, Peng Wei
School of Environmental Science and Engineering, Chang'an University Xi'an 710064 China.
Key Laboratory of Subsurface Hydrology and Ecological Effect in Arid Region of Ministry of Education, Chang'an University No. 126 Yanta Road, Yanta District Xi'an 710064 China.
RSC Adv. 2019 May 7;9(25):13968-13980. doi: 10.1039/c9ra01906e.
Inherent protein conformational flexibility is important for biomolecular recognition, but this critical property is often neglected in several studies. This event can lead to large deviations in the research results. In the current contribution, we disclose the effects of the local conformational flexibility on receptor recognition by using an atomic-scale computational method. The results indicated that both static and dynamic reaction modes have noticeable differences, and these originated from the structural features of the protein molecules. Dynamic interaction results displayed that the structural stability and conformational flexibility of the proteins had a significant influence on the recognition processes. This point related closely to the characteristics of the flexible loop regions where bixin located within the protein structures. The energy decomposition analyses and circular dichroism results validated the rationality of the recognition studies. More importantly, the conformational and energy changes of some residues around the bixin binding domain were found to be vital to biological reactions. These microscopic findings clarified the nature of the phenomenon that the local conformational flexibility could intervene in receptor recognition. Obviously, this report may provide biophysical evidence for the exploration of the structure-function relationships of the biological receptors in the human body.
蛋白质固有的构象灵活性对于生物分子识别很重要，但这一关键特性在一些研究中常常被忽视。这种情况可能导致研究结果出现较大偏差。在本论文中，我们使用原子尺度的计算方法揭示了局部构象灵活性对受体识别的影响。结果表明，静态和动态反应模式存在显著差异，这些差异源自蛋白质分子的结构特征。动态相互作用结果显示，蛋白质的结构稳定性和构象灵活性对识别过程有重大影响。这一点与蛋白质结构中胭脂树素所在的柔性环区域的特征密切相关。能量分解分析和圆二色性结果验证了识别研究的合理性。更重要的是，发现胭脂树素结合域周围一些残基的构象和能量变化对生物反应至关重要。这些微观发现阐明了局部构象灵活性能够干预受体识别这一现象的本质。显然，本报告可能为探索人体生物受体的结构 - 功能关系提供生物物理证据。
