α-晶状体蛋白：对均一四级结构的探索。
Alpha crystallin: the quest for a homogeneous quaternary structure.
作者信息
Horwitz Joseph
机构信息
Jules Stein Eye Institute, UCLA School of Medicine, Los Angeles, CA 90095-7008, USA.
出版信息
Exp Eye Res. 2009 Feb;88(2):190-4. doi: 10.1016/j.exer.2008.07.007. Epub 2008 Jul 25.
Abstract
Alpha A and alpha B crystallins are key members of the small heat-shock protein family. In addition to being a major structural protein of the lens, they are constitutively found in many other cells, where their function is not completely understood. Alpha B crystallin is also known to be over-expressed in many neurological diseases. To date, all efforts to crystallize alpha A or alpha B have failed. Thus, high-resolution data on the tertiary and quaternary structures of alpha crystallin is not available. The main reason for this failure seems to be the polydisperse nature of alpha crystallin. This review deals mainly with the polydisperse properties of alpha crystallin and the influence of post-translational modification, chemical modifications, truncations and mutation on its quaternary structure.
摘要
αA晶体蛋白和αB晶体蛋白是小分子热休克蛋白家族的关键成员。除了作为晶状体的主要结构蛋白外，它们还存在于许多其他细胞中，但其功能尚未完全明确。已知αB晶体蛋白在许多神经疾病中过度表达。迄今为止，所有结晶αA或αB的努力均告失败。因此，尚无关于α晶体蛋白三级和四级结构的高分辨率数据。这种失败的主要原因似乎是α晶体蛋白的多分散性质。本综述主要探讨α晶体蛋白的多分散特性以及翻译后修饰、化学修饰、截短和突变对其四级结构的影响。
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