Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri.
Protein Sci. 2019 Apr;28(4):837-842. doi: 10.1002/pro.3583. Epub 2019 Feb 18.
It has been estimated that 30%-50% of proteins self-assemble to form complexes consisting of multiple copies of themselves. If there is a functional difference between different molecular weight forms and if these forms interconvert on a reasonable time scale then oligomerization could be an important metabolic control mechanism. The example given here is of apoE for which the oligomerization process is measured in minutes to hours and the monomer binds lipids while the tetramer does not. Examination of the literature reveals few reports on the rate constants that control the interconversion of different molecular weight forms. Perhaps it is time to collect such data.
据估计，有 30%-50%的蛋白质会自我组装，形成由多个自身拷贝组成的复合物。如果不同分子量形式之间存在功能差异，并且这些形式在合理的时间尺度上相互转化，那么寡聚化可能是一种重要的代谢控制机制。这里给出的例子是载脂蛋白 E（apoE），其寡聚化过程在几分钟到几小时之间，单体结合脂质，而四聚体则不结合。文献检查显示，关于控制不同分子量形式相互转化的速率常数的报告很少。也许现在是时候收集这些数据了。
