• 主题
高级搜索  >
历史搜索 清空历史
首页> 美国卫生研究院文献>Protein Science : A Publication of the Protein Society >Disordered linkers in multidomain allosteric proteins: Entropic effect to favor the open state or enhanced local concentration to favor the closed state?
【2h】

Disordered linkers in multidomain allosteric proteins: Entropic effect to favor the open state or enhanced local concentration to favor the closed state?

机译：多域变构蛋白中的无序接头：熵效应有利于开放状态还是增强局部浓度有利于封闭状态？

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

There are many multidomain allosteric proteins where an allosteric signal at the allosteric domain modifies the activity of the functional domain. Intrinsically disordered regions (linkers) are widely involved in this kind of regulation process, but the essential role they play therein is not well understood. Here, we investigated the effect of linkers in stabilizing the open or the closed states of multidomain proteins using combined thermodynamic deduction and coarse‐grained molecular dynamics simulations. We revealed that the influence of linker can be fully characterized by an effective local concentration [B]0. When K d is smaller than [B]0, the closed state would be favored; while the open state would be preferred when K d is larger than [B]0. We used four protein systems with markedly different domain–domain binding affinity and structural order/disorder as model systems to understand the relationship between [B]0 and the linker length as well as its flexibility. The linker length is the main practical determinant of [B]0. [B]0 of a flexible linker with 40–60 residues was determined to be in a narrow range of 0.2–0.6 mM, while a too short or too long length would dramatically decrease [B]0. With the revealed [B]0 range, the introduction of a flexible linker makes the regulation of weakly interacting partners possible.
机译：有许多多域变构蛋白，其中变构域的变构信号会修饰功能域的活性。内在无序的区域（连接子）广泛参与这种调节过程，但人们对其所起的基本作用尚不甚了解。在这里，我们结合热力学推导和粗粒度分子动力学模拟研究了接头在稳定多域蛋白的开放或闭合状态中的作用。我们发现，接头的影响可以通过有效的局部浓度[B] 0来完全表征。当K d小于[B] 0时，将处于关闭状态；而当K d大于[B] 0时，打开状态将是首选。我们使用具有明显不同的结构域-结构域结合亲和力和结构有序/无序的四种蛋白质系统作为模型系统，以了解[B] 0与接头长度之间的关系及其灵活性。接头长度是[B] 0的主要实际决定因素。确定具有40–60个残基的柔性接头的[B] 0处于0.2-0.6 mM的狭窄范围内，而太短或太长的长度则会显着降低[B] 0。随着[B] 0范围的揭示，灵活连接子的引入使得弱相互作用伙伴的调控成为可能。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

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