Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR.
Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR.
复制标题
通过磷 31 NMR 探测蛋白质磷酸化对 SLBP-组蛋白 mRNA 复合物结合诱导折叠的贡献。
DOI：
10.1016/j.fob.2014.10.002
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发表时间：
2014
期刊：
影响因子：
2.6
通讯作者：
Thapar,Roopa
中科院分区：
文献类型：
--
作者：
Thapar,Roopa
磷-31(31P)核磁共振可用于表征磷酸化蛋白质的结构和动力学。在这里，我使用31P核磁共振来报告位于SLBP(茎环结合蛋白)的RNA结合域中的磷苏氨酸的化学性质。SLBP是一种本质上无序的蛋白质，苏氨酸的磷酸化促进了SLBP-RNA复合体的组装。数据表明，31P化学位移可以作为一个很好的光谱探针，用于研究固有无序蛋白质中磷酸盐偶联的折叠和结合过程，特别是当磷酸盐表现出扭转应变并参与氢键相互作用网络的时候。
Phosphorus-31 (31P) NMR can be used to characterize the structure and dynamics of phosphorylated proteins. Here, I use31P NMR to report on the chemical nature of a phosphothreonine that lies in the RNA binding domain of SLBP (stem-loop binding protein). SLBP is an intrinsically disordered protein and phosphorylation at this threonine promotes the assembly of the SLBP–RNA complex. The data show that the31P chemical shift can be a good spectroscopic probe for phosphate-coupled folding and binding processes in intrinsically disordered proteins, particularly where the phosphate exhibits torsional strain and is involved in a network of hydrogen-bonding interactions.