直接监测丝裂原活化蛋白激酶 p38α 激活环的构象平衡。
Direct monitoring of the conformational equilibria of the activation loop in the mitogen-activated protein kinase p38α.
机构信息
Department of Chemistry and Konstanz Research School Chemical Biology, (KoRS-CB), University of Konstanz, Universitätsstraße 10, 78457 Konstanz, Germany.
出版信息
Chem Commun (Camb). 2018 Oct 23;54(85):12057-12060. doi: 10.1039/c8cc06128a.
Conformational transitions in protein kinases are crucial for the biological function of these enzymes. Here, we characterize and assess conformational equilibria of the activation loop and the effect of small molecule inhibitors in the MAP kinase p38α. Our work experimentally revealed the existence of a two-state equilibrium for p38α while the addition of inhibitors shifts the equilibrium between these two states.
构象转变在蛋白激酶的生物学功能中至关重要。在这里，我们对 MAP 激酶 p38α 的激活环构象平衡和小分子抑制剂的作用进行了表征和评估。我们的工作实验揭示了 p38α 的二态平衡的存在，而抑制剂的加入则改变了这两种状态之间的平衡。
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