通过对兔朊病毒野生型和突变体的分子动力学模拟研究其结构稳定性。
Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants.
机构信息
Victorian Life Sciences Computation Initiative, The University of Melbourne, 1 Hull Road, Croydon, VIC 3136, Australia.
出版信息
J Theor Biol. 2010 May 7;264(1):119-22. doi: 10.1016/j.jtbi.2010.01.024. Epub 2010 Jan 28.
Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect humans and animals. Rabbits are the only mammalian species reported to be resistant to infection from prion diseases isolated from other species (Vorberg et al., 2003). Fortunately, the NMR structure of rabbit prion (124-228) (PDB entry 2FJ3), the NMR structure of rabbit prion protein mutation S173N (PDB entry 2JOH) and the NMR structure of rabbit prion protein mutation I214V (PDB entry 2JOM) were released recently. This paper studies these NMR structures by molecular dynamics simulations. Simulation results confirm the structural stability of wild-type rabbit prion, and show that the salt bridge between D177 and R163 greatly contributes to the structural stability of rabbit prion protein.
朊病毒病是一种具有传染性的、不可治愈的神经退行性疾病，可感染人类和动物。兔是唯一被报道对从其他物种分离得到的朊病毒病具有抗性的哺乳动物物种（Vorberg 等人，2003 年）。幸运的是，最近公布了兔朊病毒（124-228）（PDB 条目 2FJ3）、兔朊病毒蛋白突变 S173N（PDB 条目 2JOH）和兔朊病毒蛋白突变 I214V（PDB 条目 2JOM）的 NMR 结构。本文通过分子动力学模拟研究了这些 NMR 结构。模拟结果证实了野生型兔朊病毒的结构稳定性，并表明 D177 和 R163 之间的盐桥对兔朊病毒蛋白的结构稳定性有很大贡献。
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