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.

中文翻译：

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人类小热休克蛋白的结构方面与其功能活动相关。


小热休克蛋白通过以不依赖于 ATP 的方式结合未折叠底物蛋白来发挥伴侣的作用，使它们保持在可折叠状态并防止不可逆聚集。它们在以蛋白质聚集为特征的疾病中发挥着至关重要的作用，例如神经退行性疾病和神经肌肉疾病，但也与白内障、癌症和先天性疾病有关。因此，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。本综述将概述有关人类小热休克蛋白结构复杂性的现有知识，这可能有助于寻找此类治疗分子。