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首页> 外文学位 >Exploring induced secondary structure and unmethylated DNA binding domains of Methyl CpG binding protein 2 (MeCP2).
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Exploring induced secondary structure and unmethylated DNA binding domains of Methyl CpG binding protein 2 (MeCP2).

机译：探索甲基CpG结合蛋白2（MeCP2）的诱导的二级结构和未甲基化的DNA结合域。

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摘要

Our understanding of Methyl CpG binding protein 2 (MeCP2) structure and function has changed and expanded considerably over the last two decades. Mutations along the entirety of the human MeCP2 gene product lead to a disease state---Rett syndrome. The clinical connection of this protein has continued to drive intense research into the nature of MeCP2 structure and function. There is now considerable and corroborated evidence that proves MeCP2 is an archetypical intrinsically disordered protein acting as a global ATP independent chromatin architectural protein. The ubiquity of MeCP2 in vertebrate neuronal nuclei has only recently been realized and has focused my investigations. Results from my work demonstrate a clear relationship between predicted &agr;-molecular recognition features and inducible &agr;-helical structure. From these data I suggest that inducible &agr;-helices and maintained intrinsic disorder participate in binding the pool the twenty reported MeCP2 binding partners. In addition to structural studies I have identified two non-specific unmethylated DNA binding domains unreported in the literature at the onset of my work. I have also shown that MeCP2 acquires some secondary structural stability when bound to DNA and relatively little additional stability when bound to methylated DNA. The results presented here improve the fine resolution functional understanding of MeCP2 by observing isolated fragments of MeCP2 using both structural and functional methods. This approach is significant in and of itself as, like the large disordered subset of all eukaryotic proteins, the full-length MeCP2 molecule has proven impossible to crystallize thus far. Therefore narrowing the amino acid residues responsible for DNA binding activity or any other measurable functionality in a solution state is valuable.
机译：在过去的二十年中，我们对甲基CpG结合蛋白2（MeCP2）的结构和功能的了解发生了变化，并在很大程度上得到扩展。整个人类MeCP2基因产物的突变会导致疾病状态--- Rett综合征。这种蛋白质的临床联系一直在继续推动对MeCP2结构和功能性质的深入研究。现在，有大量确凿的证据证明MeCP2是一种典型的内在无序蛋白，可作为一种独立于全球ATP的染色质结构蛋白。 MeCP2在脊椎动物神经元核中的普遍存在只是最近才意识到，并集中了我的研究。我的工作结果表明，预测的-a分子识别特征与可诱导的-a螺旋结构之间存在明确的关系。从这些数据中，我建议诱导型α-螺旋和维持的内在紊乱参与结合了二十种已报道的MeCP2结合伴侣。除了结构研究之外，我还发现了我工作开始时文献中未报道的两个非特异性未甲基化DNA结合结构域。我还表明，MeCP2与DNA结合时具有一些二级结构稳定性，而与甲基化DNA结合时则具有相对较小的附加稳定性。此处提供的结果通过使用结构和功能方法观察MeCP2的分离片段，提高了对MeCP2的高分辨率功能的理解。这种方法本身具有重要意义，因为像所有真核蛋白的大型无序子集一样，到目前为止，全长MeCP2分子已被证明无法结晶。因此，缩小溶液状态下负责DNA结合活性或任何其他可测量功能的氨基酸残基很有价值。

著录项

  • 作者

    Hite, Kristopher Charles.;

  • 作者单位

    Colorado State University.;

  • 授予单位 Colorado State University.;
  • 学科 Chemistry Biochemistry.
  • 学位 Ph.D.
  • 年度 2011
  • 页码 195 p.
  • 总页数 195
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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