Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.
Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.
复制标题
DOI：
10.1016/j.str.2016.05.011
复制
发表时间：
2016-07-06
期刊：
影响因子：
--
通讯作者：
Markley JL
中科院分区：
文献类型：
--
作者：
Alderson TR;Kim JH;Markley JL
蛋白质错误折叠和聚集是对蛋白质稳态（蛋白质稳态）的维持施加显著量的压力的病理事件。为了防止和修复蛋白质的错误折叠和聚集，细胞配备了强大的机制，主要依赖于分子伴侣。两类分子伴侣，热休克蛋白70 kDa（Hsp 70）和Hsp 40，识别并结合错误折叠的蛋白质，防止其毒性生物分子聚集，并使重折叠或靶向降解。在这里，我们回顾了热休克蛋白70和热休克蛋白40-热休克蛋白70复合物的结构生物学的现状，并研究它们的结构，动力学和功能之间的联系。我们强调了核磁共振（NMR）光谱的力量，以解开分子伴侣及其作用机制背后的复杂关系。Hsp 70和Hsp 40是防止蛋白质错误折叠和聚集的分子伴侣。Alderson等综述了Hsp 70的结构和内部动力学及其与Hsp 40的相互作用。
Protein misfolding and aggregation are pathological events that place a significant amount of stress on the maintenance of protein homeostasis (proteostasis). To prevent and repair protein misfolding and aggregation, cells are equipped with robust mechanisms that mainly rely on molecular chaperones. Two classes of molecular chaperones, heat shock protein 70 kDa (Hsp70) and Hsp40, recognize and bind to misfolded proteins, preventing their toxic biomolecular aggregation and enabling refolding or targeted degradation. Here, we review the current state of structural biology of Hsp70 and Hsp40-Hsp70 complexes and examine the link between their structures, dynamics, and functions. We highlight the power of nuclear magnetic resonance (NMR) spectroscopy to untangle complex relationships behind molecular chaperones and their mechanism(s) of action. Hsp70 and Hsp40 are molecular chaperones that prevent protein misfolding and aggregation. Here, Alderson et al. review the structures and internal dynamics of Hsp70 and its interaction with Hsp40.