伴随着三性原I由原酶的蛋白质分解的构成动力学
Arjun S Adhikari1, Emerson Glassey, Alexander R Dunn
1Department of Chemical Engineering, Stanford University, Stanford, California 94305, USA.
Journal of the American Chemical Society
|June 23, 2012
概括
矩阵金属蛋白酶-1 (MMP-1) 切割拉伸的原蛋白,而克洛斯特里迪亚姆原酶切割完整的原蛋白. 这种差异解释了它们在原体降解中的独特机制和特异性.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 生物物理学的生物物理.
背景情况:
- 原酶降解原蛋白,这是发展,愈合和转移的关键过程.
- 由原酶破坏原三环螺旋的精确机制尚未完全理解.
研究的目的:
- 为了研究人类基质金属蛋白酶-1 (MMP-1) 和克洛斯特里蛋白酶的取决于力量的原体裂解机制.
- 阐明这些酶对差异性原溶解的结构基础.
主要方法:
- 使用单分子磁笔测试来对原I施加受控的力.
- 在不同的力条件下,由MMP-1和Clostridium原酶表征的原体裂变速率.
主要成果:
- 在16 pN的力下,MMP-1-介导的原分裂率增加了8倍.
- 克洛斯特 Kolagenase 分裂速率不受施加力的影响.
- 对MMP-1的异构三元原体裂变的强力敏感性低于同构三元模型.
结论:
- MMP-1可能会切割一个短暂的,拉伸的原体形状.
- 克洛斯特 Kolagenase 分裂完整的原三环,解释了强力不敏感性和广泛的特异性.
- 原蛋白结构和酶机制决定了原溶解活性和强力敏感性.
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