ニュース

「Biophysics and Physicobiology」にTeikichi Ikura et al. “Mutational effects of Cys113 on structural dynamics of Pin1”を掲載

2019年11月29日 学会から

日本生物物理学会欧文誌[Biophysics and Physicobiology]に以下の論文が新規掲載されました。

Teikichi Ikura, Yasushige Yonezawa, Nobutoshi Ito “Mutational effects of Cys113 on structural dynamics of Pin1”

【Significance】
Closed-open dynamics must be essential for PPIase activity of Pin1

Five-hundred ns of MD simulations of full-length wild-type Pin1 and C113A mutant were performed in order to elucidate why a mutation C113A drastically reduced the PPIase activity of Pin1. In the dynamics of wild-type protein, the phosphate binding loop (K63-S71) as well as the interdomain hinge showed the closed-open dynamics which correlated with the change of the hydrogen-bonding network of the dual-histidine motif. In contrast, in the dynamics of C113A mutant, the phosphate binding loop took only the closed conformation together with the interdomain hinge. Such closed-open dynamics must be essential for the PPIase activity of Pin1.

Biophysics and Physicobiology, Vol.16, 452-465
URL:https://doi.org/10.2142/biophysico.16.0_452


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