RAIDD CARD的解决方案结构和在caspase-2和caspase-9招募中CARD/CARD相互作用的模型
1Committee on Higher Degrees in Biophysics, Harvard University, Cambridge, Massachusetts 02138, USA.
Cell
|August 8, 1998
概括
雷德的卡斯帕斯招募域 (CARD) 结构显示了保留的表面极性. 这种两极性对于CARD/CARD相互作用至关重要,在细胞亡过程中调解caspase招募.
科学领域:
- 分子生物学分子生物学
- 结构生物学 结构生物学
- 细胞死亡途径 细胞死亡途径
背景情况:
- 细胞亡 (编程细胞死亡) 涉及通过同类相互作用通过适应蛋白招募caspases.
- 这些相互作用发生在适应器的卡斯帕斯招募域 (CARD) 和卡斯帕斯的原域之间.
研究的目的:
- 为了确定RAIDD适配蛋白的CARD的三维结构.
- 阐明卡斯巴酶招募中的CARD/CARD相互作用的分子机制.
主要方法:
- 使用X射线晶体学来解决RAIDD适应蛋白的CARD结构.
- 采用同质模型来预测ICH-1 CARD的结构.
- 进行了变异性研究,以调查表面贴片在CARD/CARD相互作用中的作用.
主要成果:
- RAIDD CARD结构包括六个螺旋,在拓上与Fas死亡域相似.
- 袭击卡的表面呈现出明显的基本和酸性补丁.
- 这些表面极性被保存在ICH-1 CARD中,并介于RAIDD和ICH-1之间的相互作用.
结论:
- 突击卡的已解决结构为caspase招募的分子基础提供了洞察力.
- 在CARD中保留的基本/酸表面极性似乎是CARD/卡片相互作用的一般机制.
- 这种机制可能是各种亡相关蛋白质的基本功能,包括Apaf-1,caspase-9,Ced-4和Ced-3.
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