Structural aspects of the human small heat shock proteins related to their functional activities
Structural aspects of the human small heat shock proteins related to their functional activities
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DOI：
10.1007/s12192-020-01093-1
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发表时间：
2020-04-06
影响因子：
3.8
通讯作者：
Boelens, Wilbert C.
中科院分区：
文献类型：
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作者：
Boelens, Wilbert C.
小的热休克蛋白通过以ATP非依赖性方式结合解折叠底物蛋白以保持它们处于折叠能力状态并防止不可逆聚集而起伴侣作用。它们在以蛋白质聚集为特征的疾病中发挥关键作用，例如神经退行性疾病和神经肌肉疾病，但也涉及白内障，癌症和先天性疾病。出于这个原因，这些蛋白质是寻找可能影响伴侣活性或补偿特定突变的分子的有趣的治疗靶点。本文综述了人类小分子热休克蛋白的结构复杂性，这可能有助于寻找这样的治疗分子。
Small heat shock proteins function as chaperones by binding unfolding substrate proteins in an ATP-independent manner to keep them in a folding-competent state and to prevent irreversible aggregation. They play crucial roles in diseases that are characterized by protein aggregation, such as neurodegenerative and neuromuscular diseases, but are also involved in cataract, cancer, and congenital disorders. For this reason, these proteins are interesting therapeutic targets for finding molecules that could affect the chaperone activity or compensate specific mutations. This review will give an overview of the available knowledge on the structural complexity of human small heat shock proteins, which may aid in the search for such therapeutic molecules.