Center for Integrated Protein Science Munich CIPSM at the Department Chemie, Technische Universität München, Garching, Germany.
Center for Integrated Protein Science Munich CIPSM at the Department Chemie, Technische Universität München, Garching, Germany.
Adv Protein Chem Struct Biol. 2019;114:1-60. doi: 10.1016/bs.apcsb.2018.10.001. Epub 2018 Dec 1.
To be able to perform their biological function, a protein needs to be correctly folded into its three dimensional structure. The protein folding process is spontaneous and does not require the input of energy. However, in the crowded cellular environment where there is high risk of inter-molecular interactions that may lead to protein molecules sticking to each other, hence forming aggregates, protein folding is assisted. Cells have evolved robust machinery called molecular chaperones to deal with the protein folding problem and to maintain proteins in their functional state. Molecular chaperones promote efficient folding of newly synthesized proteins, prevent their aggregation and ensure protein homeostasis in cells. There are different classes of molecular chaperones functioning in a complex interplay. In this review, we discuss the principal characteristics of different classes of molecular chaperones, their structure-function relationships, their mode of regulation and their involvement in human disorders.
为了发挥其生物功能，蛋白质需要正确折叠成其三维结构。蛋白质折叠过程是自发的，不需要能量输入。然而，在拥挤的细胞环境中，分子间相互作用的风险很高，可能导致蛋白质分子相互黏附，从而形成聚集体，因此需要辅助蛋白质折叠。细胞已经进化出一种叫做分子伴侣的强大机制来处理蛋白质折叠问题，并维持蛋白质处于其功能状态。分子伴侣促进新合成蛋白质的有效折叠，防止其聚集，并确保细胞内蛋白质的平衡。有不同类型的分子伴侣在复杂的相互作用中发挥作用。在这篇综述中，我们讨论了不同类型分子伴侣的主要特征、它们的结构-功能关系、它们的调节方式以及它们在人类疾病中的参与。
