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題名 | 以核磁共振光譜研究的磷酸水解酶抑制蛋白的結構=Structural Study on the Inhibitor Proteins of Protein Phosphatase 1 by NMR |
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作者姓名(中文) | 唐子鈞; 錢嘉琳; | 書刊名 | 化學 |
卷期 | 65:1 2007.03[民96.03] |
頁次 | 頁35-43 |
分類號 | 368.6 |
關鍵詞 | 核磁共振光譜; 磷酸水解; 蛋白質; 結構; Nuclear magnetic resonance spectroscopy; Proteins; Structure; Protein phosphatase; |
語文 | 中文(Chinese) |
中文摘要 | 本文將討論如何利用多維核磁共振光譜判定蛋白質化學位移並推測出其可能的二維結構,這些資料將可提供蛋白質與其結合蛋白質間作用機制的重要參考資料。我們將以第一型抑制蛋白為例闡述。 |
英文摘要 | Human inhibitor 1 is a heat- and acid- stable phosphor-protein, which regulates a diversity of cellular processes through the inhibition of protein phosphatase 1 (PP1). After phosphorylation of Thr35 by protein kinase A, human inhibitor 1 is converted into a potent inhibitor of protein phosphatase 1. In order to gain insight to the interaction between inhibitor-1 and PP1, we have used multidimensional heteronuclear NMR techniques to elucidate the structural properties of inhibitor-1. We have assigned full resonances of inhibitor 1. The secondary short helices spanning from 2428, 81-86, 103-109, and 127-131. These structural data can provide as a model to predict the interaction of protein phosphatase and its endogeneous inhibitor proteins. |
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