• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >An Arg/Lys-rich core peptide mimics TRBP binding to the HIV-1 TAR RNA upper-stem/loop
【24h】

An Arg/Lys-rich core peptide mimics TRBP binding to the HIV-1 TAR RNA upper-stem/loop

机译：富含Arg / Lys的核心肽模拟TRBP与HIV-1 TAR RNA上柄/环的结合

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

TRBP is a cellular protein that binds to the HIV-1 leader RNA, TAR. Circular dichroism experiments have shown that a 24 amino acid peptide (TR1), located within a dsRNA binding domain (dsRBD) of TRBP, binds TAR with a 3:1 stoichiometry, eliciting a conformational change involving base unstacking. The binding characteristics of synthetic structural variants of TAR indicate that guanine residues play a key role in the TR1-RNA interaction and that binding sites exist in the upper-stem/loop and lower stem region of TAR. Deletion analysis of TR1 has led to the identification of a 15 amino acid subpeptide (TR13) which is necessary and sufficient to bind to the high affinity upper-stem/loop binding site of TAR. Alanine scanning of TR13 has revealed that mutations in either Lys or Arg residues result in altered TAR-binding, and molecular modelling/docking experiments have shown that the two Arg residues of TR13 can interact with two appropriately spaced guanine residues in the upper-stem/loop of TAR. The TR13 lysine residues appear to be essential for maintaining structural integrity and the correct positioning of the Arg side-chains. We propose that TRBP binds TAR by means of a "2-G hook" motif and that the binding specificity of this particular member of the family of double-stranded RNA-binding proteins lies within the highly conserved dsRBD core motif. Finally, our results also suggest that TRBP may function in vivo by modifying the tertiary structure of TAR RNA. (C) 1998 Academic Press. [References: 62]
机译：TRBP是一种细胞蛋白，可与HIV-1前导RNA TAR结合。圆二色性实验表明，位于TRBP的dsRNA结合结构域（dsRBD）内的24个氨基酸的肽（TR1）以3：1的化学计量比结合TAR，引发涉及碱基堆积的构象变化。 TAR的合成结构变体的结合特征表明，鸟嘌呤残基在TR1-RNA相互作用中起关键作用，并且结合位点存在于TAR的上茎/下环和下茎区域。 TR1的缺失分析已导致鉴定出15个氨基酸的亚肽（TR13），这对于与TAR的高亲和力上位/环结合位点结合是必需的。丙氨酸对TR13的扫描显示，Lys或Arg残基中的突变会导致TAR结合发生改变，并且分子建模/对接实验表明，TR13的两个Arg残基可以与茎干中的两个适当间隔的鸟嘌呤残基相互作用。 TAR循环。 TR13赖氨酸残基似乎对于维持结构完整性和Arg侧链的正确定位至关重要。我们提出TRBP通过“ 2-G钩”基序结合TAR，并且该双链RNA结合蛋白家族的这个特定成员的结合特异性位于高度保守的dsRBD核心基序内。最后，我们的结果还表明TRBP可能通过修饰TAR RNA的三级结构在体内发挥作用。 （C）1998年学术出版社。 [参考：62]

著录项

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