The effect of PKA-phosphorylation on the structure of inhibitor-1 studied by NMR spectroscopy

Yi Choang Huang, Yi Chen Chen, Huey Jen Tsay, Chia Lin Chyan, Chun Yu Chen, Hsien Bin Huang*, Ta Hsien Lin

*此作品的通信作者

研究成果: Article同行評審

7 引文 斯高帕斯(Scopus)

摘要

Inhibitor-1 is an acid- and heat-stable protein. It can be turned into a potent inhibitor of protein phosphatase-1 (PP1) after phosphorylation at Thr35 by c-AMP-dependent protein kinase (PKA). Although it has been known that pre-phosphorylation is essential for inhibition of PP1, the structure-function relationship of Thr 35-phosphorylated inhibitor-1, such as whether or not PKA-phosphorylation pre-triggers conformational changes in inhibitor-1, remains unclear. In this study, we performed structural characterization of Thr 35-phosphoroylated inhibitor-1 by using multi-dimensional heternuclear NMR spectroscopy. The result of structural comparison between Thr 35-phosphoroylated and non-phosphorylated inhibitor-1 indicated that PKA-phosphorylation has no significant effect on the global conformation of free-state inhibitor-1. This finding may support the inference that regulation of the interactions between inhibitor-1 and PP1 through PKA-phosphorylation mainly depends on the phosphate group instead of phosphorylation-induced conformational change.

原文English
頁(從 - 到)273-278
頁數6
期刊Journal of Biochemistry
147
發行號2
DOIs
出版狀態Published - 2月 2010

指紋

深入研究「The effect of PKA-phosphorylation on the structure of inhibitor-1 studied by NMR spectroscopy」主題。共同形成了獨特的指紋。

引用此