在S100A12中介于的静态和动态:对S100蛋白质对目标识别的影响
Qian Wang1, Christopher DiForte1,2, Aleksey Aleshintsev1,2
1Department of Chemistry, College of Staten Island, City University of New York, New York, United States.
Protein science : a publication of the Protein Society
|March 19, 2024
概括
结合与S100A12的结合
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 分子生物物理学 分子生物物理学
背景情况:
- 包括S100A12在内的S100蛋白质受两个结合的EF手动图案的调节.
- 了解这些基因之间的相互作用对于破译蛋白质功能至关重要.
研究的目的:
- 调查S100A12.12中两个结位之间的合作关系.
- 用NMR光谱学和分子动力学绘制目标结合部位的全变化图.
主要方法:
- 溶液状态NMR光谱法用于研究野生型S100A12及其突变 (N63A,E31A).
- 分析包括骨干化学转移和胺放松率 (R1,R2,15N-{1H} NOE).
- 用分子动力学 (MD) 模拟来补充实验数据.
主要成果:
- 与EF-II循环的结合是转换到"开放"状态的主要触发因素.
- 单独的EF-I环结合的影响很小,但在EF-II结合时会调节动态.
- 消除EF-II结合会显著降低EF-I亲和力,并保持"封闭"的形状.
结论:
- 与S100A12结合的显示了EF-I和EF-II循环之间的合作.
- EF-II循环是功能"开放"形状的主要驱动因素.
- S100A12的动力学是全质调节,影响目标识别.
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