A POSSIBLE STRUCTURE FOR ALPHA-CRYSTALLIN
A POSSIBLE STRUCTURE FOR ALPHA-CRYSTALLIN
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DOI：
10.1016/0014-5793(87)80180-1
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发表时间：
1987-09-28
期刊：
影响因子：
3.5
通讯作者：
KORETZ, JF
中科院分区：
文献类型：
--
作者：
AUGUSTEYN, RC;KORETZ, JF
α-晶状体蛋白是哺乳动物眼睛晶状体的主要蛋白质，在体内以多聚体形式存在，由两个密切相关的亚基组成，其摩尔比因物种而异。试图确定聚合体中子单元的排列，甚至确定聚合体的大小和组成聚合体的子单元的数量，但尚未达成普遍共识。由于 λ-晶状体蛋白粒径的可变性、该参数对某些环境因素（例如温度）的明显依赖性、对任一 α-晶状体蛋白亚型的聚集没有特定要求，以及强疏水性区域和强亲水性区域之间氨基酸序列的明确划分，表明 α-晶状体蛋白聚集体具有蛋白质胶束的特性。该假设与已知的 α-晶状体蛋白分子和聚集体一致，并且可以通过实验进行测试。如果这个假设被证明是正确的，那么α-晶状体蛋白将成为天然存在的蛋白质胶束的第一个例子。
α‐Crystallin, the major protein of the mammalian eye lens, is found in vivo as a multimeric aggregate composed of two closely related subunits whose molar ratio is widely variable from species to species. Attempts to determine the arrangement of the subunits within the aggregate, or even to determine the size of the aggregate and the number of subunits composing it, have not resulted in general agreement. Because of the variability in λ‐crystallin particle size, the apparent dependence of this parameter on certain environmental factors (e.g. temperature), the absence of a specific requirement for either α‐crystallin isoform in aggregation, and the sharp division in the amino acid sequence between a strong hydrophobic region and a sharply hydrophilic one, it is suggested that the α‐crystallin aggregate has the properties of a protein micelle. This hypothesis is consistent with what is known of the α‐crystallin molecule and aggregate, and can be tested experimentally. If this hypothesis is shown to be true, then α‐crystallin will be the first example of a naturally occurring protein micelle.