热休克蛋白70（Hsp70）及热休克蛋白70-热休克蛋白40（Hsp70-Hsp40）复合物的动态结构
Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.
作者信息
Alderson Thomas Reid, Kim Jin Hae, Markley John Lute
机构信息
Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3TA, UK; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
National Magnetic Resonance Facility at Madison, Biochemistry Department, University of Wisconsin-Madison, Madison, WI 53706, USA.
出版信息
Structure. 2016 Jul 6;24(7):1014-30. doi: 10.1016/j.str.2016.05.011. Epub 2016 Jun 23.
Protein misfolding and aggregation are pathological events that place a significant amount of stress on the maintenance of protein homeostasis (proteostasis). For prevention and repair of 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 spectroscopy to untangle complex relationships behind molecular chaperones and their mechanism(s) of action.
蛋白质错误折叠和聚集是病理事件，会给蛋白质稳态（蛋白质平衡）的维持带来巨大压力。为了预防和修复蛋白质错误折叠和聚集，细胞具备了主要依赖分子伴侣的强大机制。两类分子伴侣，即70 kDa热休克蛋白（Hsp70）和Hsp40，能够识别并结合错误折叠的蛋白质，防止其形成有毒的生物分子聚集体，并促使其重新折叠或靶向降解。在此，我们综述了Hsp70以及Hsp40-Hsp70复合物的结构生物学现状，并探讨它们的结构、动力学和功能之间的联系。我们强调了核磁共振波谱在理清分子伴侣背后复杂关系及其作用机制方面的强大能力。
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