Structural analysis of the protein phosphatase 1 docking motif: Molecular description of binding specificities identifies interacting proteins
Structural analysis of the protein phosphatase 1 docking motif: Molecular description of binding specificities identifies interacting proteins
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DOI：
10.1016/j.chembiol.2005.10.009
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发表时间：
2006-01-01
影响因子：
--
通讯作者：
Enz, R
中科院分区：
文献类型：
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作者：
Meiselbach, H;Sticht, H;Enz, R
激酶和磷酸酶之间的相互作用代表了生物系统中的基本调节机制。由于磷酸酶的数量少于激酶，因此通过获得多种结合伴侣来增加其多样性，从而形成大量全酶。与蛋白磷酸酶1（PP1）相互作用的蛋白质通常通过所谓的对接基序结合以调节其酶活性、底物特异性和亚细胞定位。在这里，我们系统地确定了介导PP1相互作用蛋白的结合特异性的结构元件，并提出了一个精致的高亲和力PP1配体的共识序列。应用这种模式的数据库搜索，我们预测和实验证实了几个以前未知的PP1相互作用。因此，建议的PP1对接基序能够高度特异性预测PP1结合伴侣，从而促进全基因组识别PP1相互作用。
The interplay between kinases and phosphatases represents a fundamental regulatory mechanism in biological systems. Being less numerous than kinases, phosphatases increase their diversity by the acquisition of a variety of binding partners, thereby forming a large number of holoenzymes. Proteins interacting with protein phosphatase 1 (PP1) often bind via a so-called docking motif to regulate its enzymatic activity, substrate specificity, and subcellular localization. Here, we systematically determined structural elements that mediate the binding specificity of PP1 interacting proteins, and propose a refined consensus sequence for high-affinity PP1 ligands. Applying this pattern to database searches, we predicted and experimentally confirmed several previously unknown PP1 interactors. Thus, the suggested PP1 docking motif enables a highly specific prediction of PP1 binding partners, thereby facilitating the genome-wide identification of PP1 interactors.