HSP70分子伴侣系统研究进展

综述了HSP70分子伴侣系统的晶体结构、功能及作用机理方面的研究进展.HSP70分子伴侣能够帮助细胞内新生蛋白的折叠和跨膜运输、蛋白质多聚体结构的装配和解装配，并能在胁迫下维持蛋白质的特殊构象，防止未折叠的蛋白质变性和使聚集的蛋白质溶解复性.所有这些活性均依赖于ATP调节的HSP70与底物蛋白中的疏水片段的相互作用.

The HSP70 Molecular Chaperone System

HSP70 molecular chaperone participate in various cellular processes under normal and stress conditions, including the folding of nascent polypeptides, assembly and disassembly of multimeric protein structures, membrane translocation of secreted proteins and protein degradation. All of these activities rely on the ATP-regulated association of HSP70 with short hydrophobic segments in substrate polypeptides. Significant progress has been made in the understanding of the crystal structure of the C-terminal polypeptide-binding domain and the ATP-dependent mechanisms of HSP70.