Phosphorylation-induced conformational change responsible for the function of a myosin phosphatase inhibitor, CPI-17

Shin-ya Ohki; Masumi Eto; Rei Takada; Masato Shimizu; David L. Brautigan; Masatsune Kainosho

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Phosphorylation-induced conformational change responsible for the function of a myosin phosphatase inhibitor, CPI-17

机译：磷酸化诱导的构象变化负责肌球蛋白磷酸酶抑制剂CPI-17的功能

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摘要

The structures of CPI-17 (Protein kinase-C dependent protein phosphatase-1 (PP1) inhibitor of 17 kDa) in an inactive and an active form have been determined by multidimensional NMR spectroscopy. Comparison of the two structures revealed how the molecular switch turns on at atomic resolution. Using the NMR structure of CPI-17 in the active form, the binding with catalytic domain of PP1 (PP1c) was simulated and the binding model is proposed in this report. When the phospho-Thr38 docks to the catalytic site of PP1, possible interactions for the tight binding are found; one is electrostatic interaction between a negatively charged cluster on phospho-CPI-17 and an acidic groove of PPlc, and the other is hydrophobic interaction between a hydrophobic surface area of phospho-CPI-17 and a hydrophobic groove of PP1c.

机译：非活性和活性形式的CPI-17（17 kDa的蛋白激酶C依赖性蛋白磷酸酶-1（PP1）抑制剂）的结构已通过多维NMR光谱法确定。两种结构的比较揭示了分子开关如何以原子分辨率开启。利用活性形式的CPI-17的NMR结构，模拟了与PP1（PP1c）催化结构域的结合，并在此报告中提出了结合模型。当磷酸Thr38停靠在PP1的催化位点时，发现可能发生紧密结合的相互作用；一个是磷酸-CPI-17上带负电荷的簇与PPlc的酸性凹槽之间的静电相互作用，另一个是磷酸-CPI-17的疏水表面积与PP1c的疏水凹槽之间的疏水相互作用。

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来源
《Science and Technology of Advanced Materials》 |2004年第3期|p.383-386|共4页
作者
Shin-ya Ohki; Masumi Eto; Rei Takada; Masato Shimizu; David L. Brautigan; Masatsune Kainosho;
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作者单位

Center for Nano Materials and Technology, Japan Advanced Institute of Science and Technology (JAIST), 1-1 Asahidai, Tatsunokuchi, Ishikawa 923-1292, Japan;

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原文格式 PDF
正文语种 eng
中图分类工程材料学;
关键词
CPI-17; PP1c; modeling; PKC; smooth muscle; purkinje cell;

机译：CPI-17;PP1c;建模;PKC;平滑肌;浦肯野细胞;

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专利

1. Phosphorylation-induced conformational change responsible for the function of a myosin phosphatase inhibitor, CPI-17 [J] . Science and technology of advanced materials . 2004,第3期

机译：磷酸化诱导的构象变化负责肌球蛋白磷酸酶抑制剂CPI-17的功能
2. Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation. [J] . Ohki S, Eto M, Kariya E, Journal of Molecular Biology . 2001,第4期

机译：肌球蛋白磷酸酶抑制剂蛋白CPI-17的溶液NMR结构显示磷酸化诱导的构象变化负责激活。
3. Phosphorylation-induced conformational switching of CPI-17 produces a potent myosin phosphatase inhibitor [J] . Eto M, Kitazawa T, Matsuzawa F, Structure . 2007,第12期

机译：磷酸化诱导的CPI-17构象转换产生有效的肌球蛋白磷酸酶抑制剂
4. Investigating changes in conformation upon binding of a potent DOT1L inhibitor responsible for selective killing of mixed lineage leukemia [C] . Roxana E. Iacob, Emma J. Chory, Alexander Federation, American Society for Mass Spectrometry Conference on Mass Spectrometry and Allied Topics . 2012

机译：研究有效DOT1L抑制剂的结合对混合谱系白血病的选择性杀死的结合作用
5. Conformational and functional changes of hemoglobin and myosin induced by pH: Functional role in fish quality. [D] . Kristinsson, Hordur Gudjon. 2002

机译：pH诱导的血红蛋白和肌球蛋白的构象和功能变化：对鱼类质量的功能作用。
6. Phosphorylation-induced conformational switching of CPI-17 produces a potent myosin phosphatase inhibitor [O] . Masumi Eto, Toshio Kitazawa, Fumiko Matsuzawa, -1

机译：磷酸化诱导的CPI-17构象转换产生有效的肌球蛋白磷酸酶抑制剂
7. Phosphorylation-Induced Conformational Switching of CPI-17 Produces a Potent Myosin Phosphatase Inhibitor [O] . Eto, Masumi, Kitazawa, Toshio, Matsuzawa, Fumiko, 2007

机译：磷酸化诱导的CPI-17构象转换产生有效的肌球蛋白磷酸酶抑制剂。

Phosphorylation-induced conformational change responsible for the function of a myosin phosphatase inhibitor, CPI-17

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