Characterization of the protein phosphatase 1-binding motifs of inhibitor-2 and DARPP-32 by surface plasmon resonance

Ta Hsien Lin, Pai Chi Tsai, Hsin Tzu Liu, Yi Chen Chen, Lan Hsin Wang, Fu Kai Hsieh, Hsien Bin Huang*

*此作品的通信作者

研究成果: Article同行評審

6 引文 斯高帕斯(Scopus)

摘要

KLHY is a short amino-acid sequence of inhibitor-2. This sequence is highly conserved with the protein phosphatase 1 (PP1)-binding consensus motif, RVXF. The role of this segment in binding with PP1 is ambiguous. By using surface plasmon resonance we have characterized its binding ability to PP1. Either site-directed mutagenesis or deletion of KLHY did not significantly affect the dissociation constant between PP1 and inhibitor-2. In comparison with DARPP-32, the deletion of KKIQF, a PP1-binding motif of DARPP-32, resulted in a remarkable reduction in its affinity with PP1. Our results suggested that, compared with the common RVXF motif, the KLHY sequence in intact inhibitor-2 binds weakly to PP1.

原文English
頁(從 - 到)697-700
頁數4
期刊Journal of Biochemistry
138
發行號6
DOIs
出版狀態Published - 12月 2005

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