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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >The putative role of some conserved water molecules in the structure and function of human transthyretin
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The putative role of some conserved water molecules in the structure and function of human transthyretin

机译：一些保存水的假定的角色分子结构和功能的人类转体基因

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摘要

Human transthyretin (hTTR) is a multifunctional protein that is involved in several neurodegenerative diseases. Besides the transportation of thyroxin and vitamin A, it is also involved in the proteolysis of apolipoprotein A1 and A beta peptide. Extensive analyses of 32 high-resolution X-ray and neutron diffraction structures of hTTR followed by molecular-dynamics simulation studies using a set of 15 selected structures affirmed the presence of 44 conserved water molecules in its dimeric structure. They are found to play several important roles in the structure and function of the protein. Eight water molecules stabilize the dimeric structure through an extensive hydrogen-bonding network. The absence of some of these water molecules in highly acidic conditions (pH <= 4.0) severely affects the interfacial hydrogen-bond network, which may destabilize the native tetrameric structure, leading to its dissociation. Three pairs of conserved water molecules contribute to maintaining the geometry of the ligand-binding cavities. Some other water molecules control the orientation and dynamics of different structural elements of hTTR. This systematic study of the location, absence, networking and interactions of the conserved water molecules may shed some light on various structural and functional aspects of the protein. The present study may also provide some rational clues about the conserved water-mediated architecture and stability of hTTR.
机译：人类转体基因(hTTR)是一个多功能的蛋白质参与了几个神经退行性疾病。运输的甲状腺素和维生素A,它是也参与蛋白质水解载脂蛋白A1β肽。分析32高分辨率x射线和中子衍射结构hTTR紧随其后分子动力学模拟研究使用一组15所选结构肯定存在44守恒的水分子二聚的结构。结构和功能的重要作用的蛋白质。通过一个广泛的二聚的结构氢键网络。这些水分子在高酸性的条件(pH值< = 4.0)严重影响界面形成氢键网络,这可能会破坏本机四聚物的结构,导致它离解。分子有助于保持几何配体结合的蛀牙。分子的取向和动态控制hTTR的不同结构元素。系统研究的位置,,网络和交互的守恒的水分子可能阐明不同蛋白质的结构和功能方面。目前的研究也提供了一些理性的对守恒water-mediated线索架构和hTTR的稳定。

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