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Structural Symmetry in Membrane Proteins.
Annual Review of Biophysics ( IF 12.4 ) Pub Date : 2015-06-23 , DOI: 10.1146/annurev-biophys-051013-023008
Lucy R Forrest 1
Affiliation  

Symmetry is a common feature among natural systems, including protein structures. A strong propensity toward symmetric architectures has long been recognized for water-soluble proteins, and this propensity has been rationalized from an evolutionary standpoint. Proteins residing in cellular membranes, however, have traditionally been less amenable to structural studies, and thus the prevalence and significance of symmetry in this important class of molecules is not as well understood. In the past two decades, researchers have made great strides in this area, and these advances have provided exciting insights into the range of architectures adopted by membrane proteins. These structural studies have revealed a similarly strong bias toward symmetric arrangements, which were often unexpected and which occurred despite the restrictions imposed by the membrane environment on the possible symmetry groups. Moreover, membrane proteins disproportionately contain internal structural repeats resulting from duplication and fusion of smaller segments. This article discusses the types and origins of symmetry in membrane proteins and the implications of symmetry for protein function.

中文翻译:

膜蛋白的结构对称性。

对称性是包括蛋白质结构在内的自然系统的共同特征。长期以来,人们一直认为水溶性蛋白质对对称结构具有很强的倾向性,并且从进化的观点出发已经合理化了这种倾向性。然而,传统上,驻留在细胞膜中的蛋白质较不适合进行结构研究,因此,人们对这一重要分子类别中对称性的普遍性和意义还不太了解。在过去的二十年中,研究人员在这一领域取得了长足的进步,这些进展为膜蛋白采用的一系列结构提供了令人兴奋的见解。这些结构性研究表明,在对称排列方面存在类似的强烈偏见,尽管膜环境对可能的对称基团施加了限制,但这种情况经常是出乎意料的,并且还是会发生。此外,膜蛋白不成比例地包含由较小片段的复制和融合产生的内部结构重复。本文讨论了膜蛋白对称性的类型和起源以及对称性对蛋白功能的影响。
更新日期:2015-06-22
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