Marianayagam Neelan J, Sunde Margaret, Matthews Jacqueline M
School of Molecular and Microbial Biosciences, University of Sydney, Sydney, NSW 2006, Australia.
Trends Biochem Sci. 2004 Nov;29(11):618-25. doi: 10.1016/j.tibs.2004.09.006.
The self-association of proteins to form dimers and higher-order oligomers is a very common phenomenon. Recent structural and biophysical studies show that protein dimerization or oligomerization is a key factor in the regulation of proteins such as enzymes, ion channels, receptors and transcription factors. In addition, self-association can help to minimize genome size, while maintaining the advantages of modular complex formation. Oligomerization, however, can also have deleterious consequences when nonnative oligomers associated with pathogenic states are generated. Specific protein dimerization is integral to biological function, structure and control, and must be under substantial selection pressure to be maintained with such frequency throughout biology.
蛋白质自我缔合形成二聚体和高阶寡聚体是一种非常普遍的现象。最近的结构和生物物理研究表明，蛋白质二聚化或寡聚化是调节酶、离子通道、受体和转录因子等蛋白质的关键因素。此外，自我缔合有助于最小化基因组大小，同时保持模块化复合物形成的优势。然而，当产生与致病状态相关的非天然寡聚体时，寡聚化也可能产生有害后果。特定的蛋白质二聚化对于生物功能、结构和调控不可或缺，并且必须承受巨大的选择压力才能在整个生物学中以如此高的频率维持。
