在亚纳米分辨率电子冷显微镜结构的异构体ABC出口商的结构
JungMin Kim1, Shenping Wu2, Thomas M Tomasiak2
1Department of Pharmaceutical Chemistry, University of California San Francisco, 600 16th Street, San Francisco, California 94158, USA.
Nature
|November 4, 2014
概括
这项研究揭示了面向内部的TmrAB ABC出口者的结构,为多药耐药性机制提供了洞察力. 了解这个传送器的理解
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:
- ATP结合盒 (ABC) 载体是关键的膜蛋白质.
- ABC出口商涉及多药耐药性和人类疾病.
研究的目的:
- 确定TmrAB ABC出口商的结构.
- 阐明TmrAB的面向内部的形状.
主要方法:
- 单粒子电子冷显微镜在亚纳米分辨率.
- 用洗剂溶解的TmrAB的结构确定.
主要成果:
- 解决了TmrAB的面向内部的,无核酸的形状.
- 确定了跨膜域中的一个可访问的腔.
- 通过carboxy-terminal螺旋体观察到核酸结合域之间的接触.
结论:
- TmrAB结构为向内面的ABC传送器提供了一个模型.
- 表明一种构造变化机制,涉及核酸结合域的滑动和旋转.
- 了解了解多药耐药传递器功能的信息.
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