• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文学位 >Molecular studies in protein/DNA recognition: Crystallographic trials of the retrovirus integrase protein and the crystal structure of the Escherichia coli response regulator NarL(C)/DNA complex.
【24h】

Molecular studies in protein/DNA recognition: Crystallographic trials of the retrovirus integrase protein and the crystal structure of the Escherichia coli response regulator NarL(C)/DNA complex.

机译：蛋白质/ DNA识别的分子研究：逆转录病毒整合酶蛋白的结晶学试验和大肠杆菌反应调节因子NarL（C）/ DNA复合物的晶体结构。

获取原文
获取原文并翻译 | 示例
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

DNA structure and recognition is critical in all life stages. However, molecular rules describing sequence-dependent DNA structure or recognition by proteins have been elusive. The efforts of this dissertation have been toward understanding the molecular recognition of DNA through x-ray crystallographic studies. Although DNA is considered the stable transcript of life, the DNA of somatic cells has been shown to transmigrate, and the storage medium of DNA is an ancient, living, dynamic substance.; Two systems have been chosen to elucidate the recognition of DNA by proteins: the retroviral integrase protein and a bacterial signal transduction pathway transcription factor. (a) The feline immunodeficiency virus integrase protein binds DNA weakly, but yet readily performs the integration reaction essential to retroviral propagation. No diffraction quality crystals were obtained. (b) The NarL transcription factor does not bind DNA until activated by phosphorylation. The NarL C-terminal DNA-binding domain alone mimics the activated protein by site-specifically binding its DNA target. Crystals were grown of the DNA target site bound to the C-terminal domain. The crystal structure showed unusual patterns of recognition and allowed DNA recognition by related proteins to be predicted. Clearly, DNA recognition is the tender balance of steric, charged and dispersive forces between a set of pre-existent DNA conformations as they assume the deformations imposed by the protein surface.
机译：DNA结构和识别在所有生命阶段都至关重要。但是，描述序列依赖性DNA结构或蛋白质识别的分子规则是难以捉摸的。本文的工作一直是通过X射线晶体学研究来理解DNA的分子识别。尽管DNA被认为是生命的稳定转录本，但已证明体细胞的DNA可以迁移，而DNA的存储介质是古老的，有生命的，动态的物质。已经选择了两个系统来阐明蛋白质对DNA的识别：逆转录病毒整合酶蛋白质和细菌信号转导途径转录因子。 （a）猫免疫缺陷病毒整合酶蛋白与DNA的结合较弱，但仍易于进行逆转录病毒繁殖所必需的整合反应。没有获得衍射品质的晶体。 （b）NarL转录因子直到被磷酸化激活才结合DNA。 NarL C端DNA结合结构域通过位点特异性结合其DNA靶标单独模拟激活的蛋白。生长了结合到C-末端结构域的DNA靶位点的晶体。晶体结构显示出异常的识别模式，并可以预测相关蛋白质的DNA识别。显然，DNA识别是一组预先存在的DNA构象之间的空间力，带电力和分散力之间的温和平衡，因为它们假定了蛋白质表面施加的变形。

著录项

  • 作者

    Maris, Ann Elizabeth.;

  • 作者单位

    University of California, Los Angeles.;

  • 授予单位 University of California, Los Angeles.;
  • 学科 Chemistry Biochemistry.
  • 学位 Ph.D.
  • 年度 2002
  • 页码 146 p.
  • 总页数 146
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物化学;
  • 关键词

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号