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- Title
The effect of PKA-phosphorylation on the structure of inhibitor-1 studied by NMR spectroscopy.
- Authors
Yi-Choang Huang; Yi-Chen Chen; Huey-Jen Tsay; Chia-lin Chyan; Chun-Yu Chen; Hsien-bin Huang; Ta-Hsien Lin
- Abstract
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 Thr35-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 Thr35-phosphoroylated inhibitor-1 by using multi-dimensional heternuclear NMR spectroscopy. The result of structural comparison between Thr35-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.
- Subjects
PHOSPHOPROTEIN phosphatases; PHOSPHORYLATION; PROTEIN kinases; NUCLEAR magnetic resonance spectroscopy; CHEMICAL reactions
- Publication
Journal of Biochemistry, 2010, Vol 147, Issue 2, p273
- ISSN
0021-924X
- Publication type
Article
- DOI
10.1093/jb/mvp178