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The origin of protein interactions and allostery in colocalization

机译:共定位中蛋白质相互作用和变构的起源

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摘要

Two fundamental principles can account for how regulated networks of interacting proteins originated in cells. These are the law of mass action, which holds that the binding of one molecule to another increases with concentration, and the fact that the colocalization of molecules vastly increases their local concentrations. It follows that colocalization can amplify the effect on one protein of random mutations in another protein and can therefore, through natural selection, lead to interactions between proteins and to a startling variety of complex allosteric controls. It also follows that allostery is common and that homologous proteins can have different allosteric mechanisms. Thus, the regulated protein networks of organisms seem to be the inevitable consequence of natural selection operating under physical laws.
机译:两种基本原理可以解释相互作用蛋白的调控网络如何起源于细胞。这些是质量作用定律,认为一个分子与另一种分子的结合随着浓度增加而增加,并且分子的共定位极大地增加了它们的局部浓度这一事实。因此,共定位可以放大对另一种蛋白质中的一种随机突变的蛋白质的影响,因此,通过自然选择,可以导致蛋白质之间的相互作用,并导致令人震惊的复杂变构控制。还得出这样的结论:变构是常见的,并且同源蛋白质可以具有不同的变构机制。因此,生物体受调节的蛋白质网络似乎是在自然法则下自然选择的必然结果。

著录项

  • 来源
    《Nature》 |2007年第7172期|983-990|共8页
  • 作者

    John Kuriyan; David Eisenberg;

  • 作者单位

    Howard Hughes Medical Institute, California Institute for Quantitative Biosciences, Department of Molecular and Cell Biology and Department of Chemistry, University of California, Berkeley, California 94720, USA;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 自然科学总论;
  • 关键词

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