素和三氨酸酸化之间的固有差异:酸三氨酸强烈喜欢高度排序的,紧的,循环形状
Anil K Pandey1, Himal K Ganguly1, Sudipta Kumar Sinha1,2
1Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, United States.
ACS chemical biology
|August 18, 2023
概括
蛋白质中血清素和氨酸残留物的酸化会导致显著的结构变化. 特别是氨酸酸化,诱导强烈的混乱到秩序的过渡,模仿普罗林.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 分子生物学分子生物学
背景情况:
- 通过酶和酶对蛋白质的酸化调节细胞功能.
- 了解酸化对结构的影响对于细胞信号传递至关重要.
- 酸化氨酸和氨酸是关键的翻译后修饰.
研究的目的:
- 为了研究氨酸和氨酸酸化的结构后果.
- 阐明和蛋白质中酸化引起的构造变化.
- 为了提供一种结构性基础,用于酸化氨酸和氨酸酸化的不同作用.
主要方法:
- 圆形二重化谱光学 圆形二重化谱光学
- 核磁共振 (NMR) 光谱学 核磁共振 (NMR) 光谱学
- 蛋白质数据库 (PDB) 的生物信息分析.
- 小分子X射线晶体学小分子X射线晶体学
- 计算的调查调查研究.
主要成果:
- 酸化氨酸和氨酸残留物会在它们的二氧化形式中诱导显著的构造限制.
- 氨酸三氨酸采用循环形状,具有受限的φ角 (∼-60°),通过非共价相互作用稳定.
- 这种三烯结构特征,模仿了普罗林的骨干循环,在各种蛋白质中观察到,包括酶激活环.
- 血清酸酸化通常会导致较小的,类似于修静态的变化,而氨酸酸化会诱导更大的,类似于步骤功能的开关.
结论:
- 酸化显著改变了蛋白质的结构和动态.
- 与索素相比,索素的独特形状偏好提供了一个独特的调节机制.
- 这些发现解释了蛋白质中氨酸和氨酸酸化位点的不同进化和利用.
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