Flexibility in the PP1:spinophilin holoenzyme.
Flexibility in the PP1:spinophilin holoenzyme.
复制标题
PP1：亲旋蛋白全酶的灵活性。
DOI：
10.1016/j.febslet.2010.11.022
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发表时间：
2011
期刊：
影响因子：
3.5
通讯作者：
Peti,Wolfgang
中科院分区：
文献类型：
--
作者：
Ragusa,MichaelJ;Allaire,Marc;Nairn,AngusC;Page,Rebecca;Peti,Wolfgang
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靶向到特定位置并调节其特异性。虽然已知许多PP1调节蛋白在未结合状态下是动态的，但对PP1全酶形成后的剩余柔韧性知之甚少。在这里，我们使用小角度x射线散射来研究PP1：嗜脊髓蛋白全酶在溶液中的柔韧性。总的来说，我们的数据表明，PP1：嗜脊髓蛋白全酶在溶液中是动态的，这允许增加嗜脊髓蛋白的捕获半径，并且可能对其生物学作用很重要。结构摘要：MINT-8057915: PP1-alpha （uniprotkb:P62136）和Spinophilin （uniprotkb:O35274）通过x射线散射（MI:0826）结合（MI:0407）
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. STRUCTURED SUMMARY: MINT-8057915: PP1-alpha (uniprotkb:P62136) and Spinophilin (uniprotkb:O35274) bind (MI:0407) by x ray scattering (MI:0826)