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一个刺自处理域的晶体结构:刺和自我拼接蛋白之间的同质性
T M Hall1, J A Porter, K E Young
1Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Cell
|October 23, 1997
概括
草虫刺蛋白 (Hh-C) 的碳氧终端域经历了自动处理. 它的晶体结构揭示了同源子域,提供了对 protein 进化和整体保护的见解.
科学领域:
- 分子生物学分子生物学
- 结构生物学 结构生物学
- 进化生物学 进化生物学
背景情况:
- 德洛索菲拉刺蛋白 (Drosophila Hedgehog protein,Hh-C) 的碳氧终端域表现出自处理活动,这对于生成活性信号形式至关重要.
- 这一过程涉及分子内部裂变和胆固醇附着在氨基末端碎片上.
研究的目的:
- 为了确定Hh-C (Hh-C17) 的活性17 kDa片段的晶体结构.
- 确定Hh-C17活性部位中的关键残留物,并阐明它们在自动处理中的作用.
- 为了探索Hh-C和intins之间的进化关系.
主要方法:
- 在Hh-C17碎片的净化和结晶.
- 进行X射线晶体学以确定Hh-C17的3D结构.
- 位点定向突变发生,以探测活性位点残留物的功能.
主要成果:
- 确定了Hh-C17的晶体结构,揭示了两个同源子域,可能源于基因重复.
- 确定了涉及子自动处理的关键活性部位残留物.
- 在Hh-C17和intins之间保留的特征表明它们具有共同的进化起源.
结论:
- Hh-C17的结构为了解子自动处理提供了分子基础.
- 这些发现表明,子蛋白域和整体之间存在可信的进化联系.
- 这项研究提供了关于蛋白质拼接机制演化的见解.
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