人类细胞周期控制酸酶的催化域的晶体结构,Cdc25A
E B Fauman1, J P Cogswell, B Lovejoy
1Department of Biological Chemistry, The University of Michigan, Ann Arbor 48109-1055, USA. fauman@umich.edu
Cell
|May 30, 1998
概括
人类Cdc25A酸酶结构揭示了一个新的折叠,与其他酸酶不同,但类似于硫转移蛋白. 这一发现为细胞循环调节和潜在的自我抑制机制提供了洞察力.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 细胞生物学 细胞生物学
背景情况:
- Cdc25酸酶是细胞分裂激酶的关键调节者.
- 了解它们的结构是解读细胞循环控制的关键.
研究的目的:
- 为了确定人类Cdc25A催化域的3D结构.
- 阐明Cdc25A酶活性和调节的结构基础.
主要方法:
- 在2.3A分辨率的X射线晶体学.
- 基于结构的序列对齐.基于结构的序列对齐.
主要成果:
- 人类Cdc25A催化域具有独特的α/β折叠,类似于罗丹,以前在酸酶中没有见过.
- 在Cys-430和Cys-384之间的二硫化键表明了潜在的氧化应激诱导的自我抑制机制.
- Asp-383扮演结构性的角色,而不是作为一般的酸;Glu-431被提议作为一般的酸.
结论:
- Cdc25A结构揭示了一个新的折叠,对酸酶分类有影响.
- 这些发现表明一种涉及氧化应激的调节机制,并确定了与MAP激酶酸酶和ACR2.2的潜在结构同质性.
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