Receiver domain structure and function in response regulator proteins.
Receiver domain structure and function in response regulator proteins.
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DOI：
10.1016/j.mib.2010.01.015
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发表时间：
2010-04
影响因子：
5.4
通讯作者：
Bourret, Robert B.
中科院分区：
文献类型：
--
作者：
Bourret, Robert B.
在双组分调节系统的信号转导过程中，传感器激酶检测和编码输入信息，而响应调节器控制输出。大多数受体结构域在反应调节器中起磷酸化介导的开关的作用，但有些在多步磷酸化继电器中转移磷酰基。受体结构域氨基酸序列的保守特征与结构相关，因此与功能相关。受体结构域在需要二价阳离子的反应中催化其自身的磷酸化和去磷酸化。分子动力学模拟补充的基础接收域开关功能的构象变化的结构调查。随着对所有受体域共享特征的理解的成熟，赋予差异的因素（例如反应速率或特异性）正在受到越来越多的关注。许多非典型或假受体域的功能没有磷酸化的例子，最近已被表征。
During signal transduction by two-component regulatory systems, sensor kinases detect and encode input information while response regulators control output. Most receiver domains function as phosphorylation-mediated switches within response regulators, but some transfer phosphoryl groups in multistep phosphorelays. Conserved features of receiver domain amino acid sequence correlate with structure and hence function. Receiver domains catalyze their own phosphorylation and dephosphorylation in reactions requiring a divalent cation. Molecular dynamics simulations are supplementing structural investigation of the conformational changes that underlie receiver domain switch function. As understanding of features shared by all receiver domains matures, factors conferring differences (e.g. in reaction rate or specificity) are receiving increased attention. Numerous examples of atypical- or pseudo-receiver domains that function without phosphorylation have recently been characterized.
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