Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI, USA.
FEBS Lett. 2011 Jan 3;585(1):36-40. doi: 10.1016/j.febslet.2010.11.022. Epub 2010 Nov 19.
Protein phosphatase 1 (PP1) interacts with ∼200 regulatory proteins to form holoenzymes, which target PP1 to specific locations and regulate its specificity. While it is known that many PP1 regulatory proteins are dynamic in the unbound state, much less is known about the residual flexibility after PP1 holoenzyme formation. Here, we have used small angle X-ray scattering to investigate the flexibility of the PP1:spinophilin holoenzyme in solution. Collectively, our data shows that the PP1:spinophilin holoenzyme is dynamic in solution, which allows for an increased capture radius of spinophilin and is likely important for its biological role.
蛋白磷酸酶 1（PP1）与约 200 种调节蛋白相互作用形成全酶，将 PP1 靶向特定位置并调节其特异性。虽然已经知道许多 PP1 调节蛋白在未结合状态下是动态的，但对于 PP1 全酶形成后剩余的灵活性知之甚少。在这里，我们使用小角度 X 射线散射来研究溶液中 PP1：spinophilin 全酶的灵活性。总的来说，我们的数据表明，PP1：spinophilin 全酶在溶液中是动态的，这允许 spinophilin 增加捕获半径，这对于其生物学作用可能很重要。
