Control by phosphorylation
Control by phosphorylation
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DOI：
10.1016/s0959-440x(96)80005-4
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发表时间：
1996-12-01
影响因子：
6.8
通讯作者：
OReilly, M
中科院分区：
文献类型：
--
作者：
Johnson, LN;OReilly, M
先前已获得结构数据的两个磷酸化和去磷酸化蛋白（糖原磷酸化酶和异柠檬酸脱氢酶）的例子证明了两种不同的控制机制。在糖原磷酸化酶中，磷酸化激活导致远端变构变化。在异柠檬酸脱氢酶中，磷酸化的抑制是通过静电阻断机制实现的，没有构象变化。在过去的一年中，已经确定了另外两种蛋白质（细胞周期蛋白激酶CDK2和酵母糖原磷酸化酶）的磷酸化和去磷酸化形式的结构。新的结果强调了磷酸氨基酸通过磷酸-精氨酸相互作用在蛋白质结构局部区域的组织中以及在促进远程构象反应中的重要性。
The two examples of phospho and dephospho proteins for which structural data were previously available (glycogen phosphorylase and isocitrate dehydrogenase) demonstrated two different mechanisms for control. In glycogen phosphorylase, activation by phosphorylation results in long-range allosteric changes. In isocitrate dehydrogenase, inhibition by phosphorylation is achieved by an electrostatic blocking mechanism with no conformational changes. During the past year, the structures of the phospho and dephospho forms of two more proteins, the cell cycle protein kinase CDK2 and yeast glycogen phosphorylase, have been determined, The new results highlight the importance of the phosphoamino acids both in the organization of local regions of protein structure through phosphate-arginine interactions and in the promotion of long-range conformational responses.